The mycota VIII, biology of the fungal cell 2nd ed k esser, r howard (springer, 2007)

The Mycota Edited by K Esser The Mycota I Growth, Differentiation and Sexuality 1st edition ed by J.G.H Wessels and F Meinhardt 2nd edition ed by U Kües and R Fischer II Genetics and Biotechnology Ed by U Kück III Biochemistry and Molecular Biology Ed by R Brambl and G Marzluf IV Environmental and Microbial Relationships 1st edition ed by D Wicklow and B Söderström 2nd edition ed by C.P Kubicek and I.S Druzhinina V Plant Relationships 1st edition ed by G Carroll and P Tudzynski 2nd edition ed by H.B Deising VI Human and Animal Relationships 1st edition ed by D.H Howard and J.D Miller 2nd edition ed by A Brakhage and P Zipfel VII Systematics and Evolution Ed by D.J McLaughlin, E.G McLaughlin, and P.A Lemke† VIII Biology of the Fungal Cell Ed by R.J Howard and N.A.R Gow IX Fungal Associations Ed by B Hock X Industrial Applications Ed by H.D Osiewacz XI Agricultural Applications Ed by F Kempken XII Human Fungal Pathogens Ed by J.E Domer and G.S Kobayashi XIII Fungal Genomics Ed by A.J.P Brown The Mycota A Comprehensive Treatise on Fungi as Experimental Systems for Basic and Applied Research Edited by K Esser VIII Biology of the Fungal Cell 2nd Edition Volume Editors: R.J Howard · N.A.R Gow With 86 Figures, in Color, and Tables 123 Series Editor Professor Dr Dr h.c mult Karl Esser Allgemeine Botanik Ruhr-Universität 44780 Bochum, Germany Tel.: +49 (234)32-22211 Fax.: +49 (234)32-14211 e-mail: Karl.Esser@rub.de Volume Editors Professor Dr Richard J Howard DuPont Crop Genetics Experimental Station E353 Powder Mill Road Wilmington, DE 19880-0353, USA Professor Dr Neil A.R Gow School of Medical Sciences Institute of Medical Sciences University of Aberdeen Aberdeen AB25 2ZD, UK Tel.: +1 (302)695-1494 Fax.: +1 (302)695-4509 e-mail: richard.j.howard@cgr.dupont.com Tel.: +44 (1224)555879 Fax: +44 (1224)555844 e-mail: n.gow@abdn.ac.uk Library of Congress Control Number: 2007927884 ISBN 978-3-540-70615-1 Springer Berlin Heidelberg New York ISBN 3-540-60186-4 1st ed Springer Berlin Heidelberg New York This work is subject to copyright All rights are reserved, whether the whole or part of the material is concerned, specifically the rights of translation, reprinting, reuse of illustrations, recitation, broadcasting, reproduction on microfilm or in any other way, and storage in data banks Duplication of this publication or parts thereof is permitted only under the provisions of the German Copyright Law of September 9, 1965, in its current version, and permissions for use must always be obtained from Springer-Verlag Violations are liable for prosecution under the German Copyright Law Springer is a part of Springer Science+Business Media springer.com © Springer-Verlag Berlin Heidelberg 2001, 2007 The use of general descriptive names, registered names, trademarks, etc in this publication does not imply, even in the absence of a specific statement, that such names are exempt from the relevant protective laws and regulations and therefore free for general use Editor: Dr Dieter Czeschlik, Heidelberg, Germany Desk editor: Dr Andrea Schlitzberger, Heidelberg, Germany Cover design: Erich Kirchner and WMXDesign GmbH, Heidelberg, Germany Production and typesetting: LE-TEX Jelonek, Schmidt & Vöckler GbR, Leipzig, Germany Printed on acid-free paper SPIN 11313472 31/3180 543210 Karl Esser (born 1924) is retired Professor of General Botany and Director of the Botanical Garden at the Ruhr-Universität Bochum (Germany) His scientific work focused on basic research in classical and molecular genetics in relation to practical application His studies were carried out mostly on fungi Together with his collaborators he was the first to detect plasmids in higher fungi This has led to the integration of fungal genetics in biotechnology His scientific work was distinguished by many national and international honors, especially three honorary doctoral degrees Richard J Howard (born 1952) studied hyphal growth and fungal cell structure during graduate work in the Department of Plant Pathology at Cornell University (USA) His M.S thesis (1977) focused on the role of microtubules in hyphal tip growth His Ph.D., completed in 1980, refined the technique of freeze substitution for the study of fungal cell ultrastructure He received an NSF Postdoctoral Fellowship grant in the same year and worked with the human pathogen Histoplasma capsulatum at the Barnes Hospital medical campus of Washington University in St Louis, MO (USA) In 1981 he accepted a research scientist position at the DuPont Experimental Station in Wilmington, DE (USA) where he conducted detailed studies of the rice blast pathogen Magnaporthe grisea and the cell biology of appressorium structure and function Appointed in 2003 as a Research Fellow for Crop Genetics, his laboratory now serves as the core biological imaging center for DuPont’s research and development interests Neil A.R Gow (born 1957) graduated from Edinburgh University and was a postgraduate at Aberdeen University He was a postdoctoral fellow in Denver before returning to a faculty position at Aberdeen where he now holds a personal chair in Molecular Mycology He is a founding member of the Aberdeen Fungal Group, which constitutes one of the single largest academic centres for medical mycology He is the immediate Past President of the British Mycological Society and is a Vice President of the International Society for Human and Animal Mycology and holds fellowships of the Institute of Biology, the Royal Society of Edinburgh and the American Academy of Microbiology He is currently the editor-in-chief of the journal Fungal Genetics and Biology His research interest is in the growth, morphogenesis and pathogenesis of the human fungal pathogen Candida albicans and he has specific interests in the molecular genetics of cell wall biosynthesis in fungi and the directional growth responses of fungal cells as well as the virulence properties of medically important fungal species Series Preface Mycology, the study of fungi, originated as a subdiscipline of botany and was a descriptive discipline, largely neglected as an experimental science until the early years of this century A seminal paper by Blakeslee in 1904 provided evidence for selfincompatibility, termed “heterothallism”, and stimulated interest in studies related to the control of sexual reproduction in fungi by mating-type specificities Soon to follow was the demonstration that sexually reproducing fungi exhibit Mendelian inheritance and that it was possible to conduct formal genetic analysis with fungi The names Burgeff, Kniep and Lindegren are all associated with this early period of fungal genetics research These studies and the discovery of penicillin by Fleming, who shared a Nobel Prize in 1945, provided further impetus for experimental research with fungi Thus began a period of interest in mutation induction and analysis of mutants for biochemical traits Such fundamental research, conducted largely with Neurospora crassa, led to the one gene: one enzyme hypothesis and to a second Nobel Prize for fungal research awarded to Beadle and Tatum in 1958 Fundamental research in biochemical genetics was extended to other fungi, especially to Saccharomyces cerevisiae, and by the mid-1960s fungal systems were much favored for studies in eukaryotic molecular biology and were soon able to compete with bacterial systems in the molecular arena The experimental achievements in research on the genetics and molecular biology of fungi have benefited more generally studies in the related fields of fungal biochemistry, plant pathology, medical mycology, and systematics Today, there is much interest in the genetic manipulation of fungi for applied research This current interest in biotechnical genetics has been augmented by the development of DNA-mediated transformation systems in fungi and by an understanding of gene expression and regulation at the molecular level Applied research initiatives involving fungi extend broadly to areas of interest not only to industry but to agricultural and environmental sciences as well It is this burgeoning interest in fungi as experimental systems for applied as well as basic research that has prompted publication of this series of books under the title The Mycota This title knowingly relegates fungi into a separate realm, distinct from that of either plants, animals, or protozoa For consistency throughout this Series of Volumes the names adopted for major groups of fungi (representative genera in parentheses) are as follows: Pseudomycota Division: Division: Oomycota (Achlya, Phytophthora, Pythium) Hyphochytriomycota Eumycota Division: Division: Division: Chytridiomycota (Allomyces) Zygomycota (Mucor, Phycomyces, Blakeslea) Dikaryomycota Subdivision: Ascomycotina VIII Series Preface Class: Class: Subdivision: Class: Class: Saccharomycetes (Saccharomyces, Schizosaccharomyces) Ascomycetes (Neurospora, Podospora, Aspergillus) Basidiomycotina Heterobasidiomycetes (Ustilago, Tremella) Homobasidiomycetes (Schizophyllum, Coprinus) We have made the decision to exclude from The Mycota the slime molds which, although they have traditional and strong ties to mycology, truly represent nonfungal forms insofar as they ingest nutrients by phagocytosis, lack a cell wall during the assimilative phase, and clearly show affinities with certain protozoan taxa The Series throughout will address three basic questions: what are the fungi, what they do, and what is their relevance to human affairs? Such a focused and comprehensive treatment of the fungi is long overdue in the opinion of the editors A volume devoted to systematics would ordinarily have been the first to appear in this Series However, the scope of such a volume, coupled with the need to give serious and sustained consideration to any reclassification of major fungal groups, has delayed early publication We wish, however, to provide a preamble on the nature of fungi, to acquaint readers who are unfamiliar with fungi with certain characteristics that are representative of these organisms and which make them attractive subjects for experimentation The fungi represent a heterogeneous assemblage of eukaryotic microorganisms Fungal metabolism is characteristically heterotrophic or assimilative for organic carbon and some nonelemental source of nitrogen Fungal cells characteristically imbibe or absorb, rather than ingest, nutrients and they have rigid cell walls The vast majority of fungi are haploid organisms reproducing either sexually or asexually through spores The spore forms and details on their method of production have been used to delineate most fungal taxa Although there is a multitude of spore forms, fungal spores are basically only of two types: (i) asexual spores are formed following mitosis (mitospores) and culminate vegetative growth, and (ii) sexual spores are formed following meiosis (meiospores) and are borne in or upon specialized generative structures, the latter frequently clustered in a fruit body The vegetative forms of fungi are either unicellular, yeasts are an example, or hyphal; the latter may be branched to form an extensive mycelium Regardless of these details, it is the accessibility of spores, especially the direct recovery of meiospores coupled with extended vegetative haploidy, that have made fungi especially attractive as objects for experimental research The ability of fungi, especially the saprobic fungi, to absorb and grow on rather simple and defined substrates and to convert these substances, not only into essential metabolites but into important secondary metabolites, is also noteworthy The metabolic capacities of fungi have attracted much interest in natural products chemistry and in the production of antibiotics and other bioactive compounds Fungi, especially yeasts, are important in fermentation processes Other fungi are important in the production of enzymes, citric acid and other organic compounds as well as in the fermentation of foods Fungi have invaded every conceivable ecological niche Saprobic forms abound, especially in the decay of organic debris Pathogenic forms exist with both plant and animal hosts Fungi even grow on other fungi They are found in aquatic as well as soil environments, and their spores may pollute the air Some are edible; others are poisonous Many are variously associated with plants as copartners in the formation of lichens and mycorrhizae, as symbiotic endophytes or as overt pathogens Association with animal systems varies; examples include the predaceous fungi that trap nematodes, the microfungi that grow in the anaerobic environment of the rumen, the many insectassociated fungi and the medically important pathogens afflicting humans Yes, fungi are ubiquitous and important Series Preface IX There are many fungi, conservative estimates are in the order of 100,000 species, and there are many ways to study them, from descriptive accounts of organisms found in nature to laboratory experimentation at the cellular and molecular level All such studies expand our knowledge of fungi and of fungal processes and improve our ability to utilize and to control fungi for the benefit of humankind We have invited leading research specialists in the field of mycology to contribute to this Series We are especially indebted and grateful for the initiative and leadership shown by the Volume Editors in selecting topics and assembling the experts We have all been a bit ambitious in producing these Volumes on a timely basis and therein lies the possibility of mistakes and oversights in this first edition We encourage the readership to draw our attention to any error, omission or inconsistency in this Series in order that improvements can be made in any subsequent edition Finally, we wish to acknowledge the willingness of Springer-Verlag to host this project, which is envisioned to require more than years of effort and the publication of at least nine Volumes Bochum, Germany Auburn, AL, USA April 1994 Karl Esser Paul A Lemke Series Editors Addendum to the Series Preface In early 1989, encouraged by Dieter Czeschlik, Springer-Verlag, Paul A Lemke and I began to plan The Mycota The first volume was released in 1994, 12 volumes followed in the subsequent years Unfortunately, after a long and serious illness, Paul A Lemke died in November 1995 Thus, it was my responsibility to proceed with the continuation of this series, which was supported by Joan W Bennett for Volumes X–XII The series was evidently accepted by the scientific community, because several volumes are out of print Therefore, Springer-Verlag has decided to publish completely revised and updated new editions of Volumes I, II, III, IV, V, VI, and VIII I am glad that most of the volume editors and authors have agreed to join our project again I would like to take this opportunity to thank Dieter Czeschlik, his colleague, Andrea Schlitzberger, and Springer-Verlag for their help in realizing this enterprise and for their excellent cooperation for many years Bochum, Germany February 2007 Karl Esser Network Organisation of Mycelial Fungi Barthelemy M, Barrat A, Pastor-Satorras R, Vespignani A (2005) Characterization and modeling of weighted networks Physica A 346:34–43 Bartnicki-Garcia S, Hergert F, Gierz G (1989) Computersimulation of fungal morphogenesis and the mathematical basis for hyphal (tip) growth Protoplasma 153:46–57 Bezzi M, Ciliberto A (2004) Mathematical modelling of filamentous microorganisms 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of Phanerochaete velutina: dependence on carbon availability New Phytol 142:325– 334 West GB, Brown JH, Enquist BJ (1997) A general model for the origin of allometric scaling laws in biology Science 276:122–126 West GB, Brown JH, Enquist BJ (2001) A general model for ontogenetic growth Nature 413:628–631 Westermann B, Prokisch H (2002) Mitochondrial dynamics in filamentous fungi Fungal Genet Biol 36:91–97 Xiang X, Plamann M (2003) Cytoskeleton and motor proteins in filamentous fungi Curr Opin Microbiol 6:628– 633 Yang H, King R, Reichl U, Gilles ED (1992a) Mathematicalmodel for apical growth, septation, and branching of mycelial microorganisms Biotechnol Bioeng 39:49– 58 Yang H, Reichl U, King R, Gilles ED (1992b) Measurement and simulation of the morphological development of filamentous microorganisms Biotechnol Bioeng 39:44–48 Biosystematic Index Achlya ambisexualis, 260 Achlya bisexualis, 229, 240, 244, 245 agarics, 292 Agrobacterium, 303 Albugo, 256 Allomyces macrogynus, 240 Alternaria solani, 229 Arabidopsis thaliana, 34, 75 ascomycetes, 292 Ascomycota, 28 Ashbya gossypii, 138, 143, 146, 156 Aspergillus, 51, 107, 108, 111, 258 Aspergillus flavus, 100, 103, 112 Aspergillus fumigatus, 2, 103, 104, 108–112 Aspergillus kawachii, 103 Aspergillus nidulans, 2, 4, 6, 7, 10, 11, 14, 16, 18, 22–37, 39, 59, 63, 90, 100, 103, 108, 109, 111, 112, 137, 144, 156, 157, 167, 241 Aspergillus niger, 23, 32, 103, 104, 109, 112, 145, 238, 275 Aspergillus oryzae, 51, 54, 55, 58, 63, 73, 90, 103, 112 Aureobasidium pullulans, 238 Basidiobolus microsporus, 240 basidiomycetes, 292 Basidiomycota, 25, 26, 28, 49, 50, 61, 292 Blastomyces dermatitidis, 100, 101, 107, 109 Blumeria graminis, 107, 254, 256, 257, 270 Blumeria graminis f sp hordei, 246, 265, 269, 271 Blumeria graminis f.sp avenae, 263 boletes, 292 Botryodiplodia theobromae, 260 Botrytis cinerea, 4, 6, 10, 14, 18, 22, 242, 243, 261, 268, 275 Candida, 108 Candida albicans, 32, 100, 106, 107, 109–111, 137, 138, 141, 143, 144, 167 Candida glabrata, 100, 106, 168 Candida guilliermondii, 32 Candida lusitaniae, 32 Candida tropicalis, 100 Chaetomium globosum, 4, 6, 10, 14, 18, 22 Claviceps purpurea, 274 Coccidioides immitis, 4, 6, 10, 14, 18, 22, 102, 103, 168 Cochliobolus carbonum, 275 Cochliobolus heterostrophus, 220, 257 Cochliobolus sativus, 269 Collembola, 319 Colletotrichum, 246, 247, 265, 270, 272 Colletotrichum carbonum, 276 Colletotrichum gloeosporioides, 257, 269, 273 Colletotrichum graminicola, 40, 53, 221, 246, 254, 264, 268 Colletotrichum kahawae, 266 Colletotrichum lagenarium, 257, 266 Colletotrichum lindemuthianum, 32, 222, 255, 256, 266, 268, 269, 271, 272, 275 Colletotrichum trifollii, 226, 230, 257 Coprinopsis cinerea, 297 Coprinus cinerea, 107 Coprinus sterquilinus, 311–315 Cryptococcus neoformans, 4, 6, 10, 14, 18, 22, 65, 102, 104, 105, 108–112, 171, 298 Cymadothea trifolii, 274 Debaryomyces hansenii, 107 Entamoeba, 28 Escherichia coli, 66 Eucalyptus pilularis, 70, 72 Eucalyptus seiberi, 254, 259 Exophiala (Wangiella) dermatitidis, 65, 100, 109, 245 Exophiala dermatitidis, 65, 109 Fusarium acuminatum, 100 Fusarium graminearum, 42, 109, 227, 274, 275 Fusarium oxysporum, 100, 102, 276 Fusarium sulphureum, 100 Fusarium verticillioides, 25 Geotrichum candidum, 245, 257 Giardia, 28 Gibberella zeae, 103, 107, 109, 112 Gigaspora margarita, 50, 70 Gigaspora rosea, 295 Gilbertella persicaria, 38, 39, 245 Glomus claroideum, 295 Glomus intraradices, 50, 65, 70, 74, 295, 297 Hanseniaspora osmophila, 100 Hansenula anomala, 100 Hebeloma cylindrosporum, 294 Helicobasidium mompa, 28 Heterobasidion annosum, 297 Histoplasma capsulatum, 100–102, 168 Homo sapiens, 5–10, 12–22, 26, 27, 29, 31, 32, 34–37, 39, 41 Hyaloperonospora parasitica, 255 Idriella bolleyi, 257 Kluyveromyces lactis, 100, 107 Kluyveromyces waltii, 24 Laccaria bicolor, 76, 296 332 Biosystematic Index Lotus japonicus, 295 Magnaporthe, 52 Magnaporthe grisea, 4, 6, 10, 14, 18, 22, 25, 32, 38–40, 52, 90, 103, 107, 109, 111, 112, 220, 221, 230, 238, 240, 245–247, 252, 254, 257–259, 264–266, 268 Magnaporthe poae, 269 Megacollybia platyphylla, 312 Melampsora, 265 Melampsora larici-populina, 258, 297 Melampsora lini, 264, 270–272 Metarhizium anisopliae, 230 Mucor hiemalis, 239, 241 Nectria haematococca, 63, 220, 221, 254, 256 Neolecta, 93 Neurospora, 51, 52, 72 Neurospora crassa, 4, 6, 10, 11, 14, 18, 22, 52, 62, 63, 67, 88, 100, 103, 104, 107, 109, 111, 112, 137, 138, 146, 158, 167, 227, 239, 241 Oomycota, 50, 58, 61 orchids, 292 Paracoccidioides brasiliensis, 101, 168 Paxillus involutus, 74, 75 Penicillium chrysogenum, 112 Penicillium marneffei, 100, 102, 103, 138, 146 Penicillium variotii, 109 Pestalotia malicola, 256 Phanerochaete, 49, 51, 54, 57, 58 Phanerochaete chrysosporium, 34, 298 Phanerochaete velutina, 49, 54, 55, 57, 68, 73, 311–317, 319 Phaseolus vulgaris, 272 Phialocephala fortinii, 66 Phialophora fortinii, 73 Phyllosticta ampelicida, 221, 222, 254 Phytophthora, 252, 253, 257, 260, 274 Phytophthora cinnamomi, 221, 222, 245, 252, 254, 256, 258– 260, 264 Phytophthora infestans, 226, 229, 253, 256, 275 Phytophthora nicotianae, 252, 256 Phytophthora palmivora, 224, 226, 229, 253 Phytophthora parasitica, 226 Phytophthora ramorum, 256 Phytophthora sojae, 252, 256 Pichia angusta, 107 Pichia membranaefaciens, 100 Pichia pastoris, 28, 29, 38 Pisolithus, 49–51, 54, 57, 58, 65 Pisolithus microcarpus, 49, 70, 295 Pisolithus tinctorius, 49, 52, 54, 59, 62, 66, 67, 72, 73, 76 Plasmopara, 256 Pleurotus ostreatus, 297 Puccinia, 262, 265 Puccinia arachidis, 271 Puccinia graminis f sp tritici, 263, 265 Puccinia hordei, 255, 263 Pythium, 243, 252, 256, 257 Pythium aphanidermatum, 227, 253 Pythium graminicola, 243 Pythium insidiosum, 243 Rhizoctonia, 262, 292 Rhizoctonia oryzae, 4, 6, 10, 14, 22, 31, 261 Rhizoctonia solani, 155, 321 Saccharomyces cerevisiae, 4, 6, 7, 10, 11, 14, 16, 18, 22–27, 29–37, 39, 41, 50–54, 56, 58, 60–64, 66–68, 70–76, 98, 100, 106–112, 137–143, 167 Saccharomyces rouxii, 100 Saprolegnia ferax, 62, 227, 258, 261 Schizophyllum commune, 100 Schizosaccharomyces pombe, 29, 32, 62, 63, 75, 99, 107–110, 138, 141, 144, 146, 167 Sclerotinia, 274 Sclerotinia sclerotiorum, 4, 6, 10, 14, 18, 22, 260, 265, 275 Sclerotium rolfsii, 100, 261 Sporothrix schenckii, 101, 104, 109 Thraustotheca clavata, 239, 241 Trichoderma viride, 28, 33 Tricholomataceae, 292 Trichophyton mentagrophytes, 100 Trichosporon cutaneum, 105 Trigonopsis variabilis, 100 truffles, 292 Uncinula necator, 256 Uromyces, 265, 272 Uromyces appendiculatus, 221, 254, 263–266 Uromyces fabae, 52, 254, 256, 269, 272, 273 Uromyces phaseoli, 62 Uromyces viciae-fabae, 255 Uromyces vignae, 269 Ustilago maydis, 26, 32, 37, 42, 52–54, 61–63, 104–106, 108– 111, 297 Vicia faba, 255, 269 Wangiella dermatitidis, 245 Xenopus, 273 Yarrowia lipolytica, 106 Zoophthora radicans, 230 Zygomycota, Subject Index 14 C-aminoisobutyrate, 325 5-deoxy-strigol, 295 a1-α2 complex, 207 acridine orange, 51 actin, 26, 34, 37, 38, 63, 142, 185, 258 actomyosin ring, 140–142, 149, 150 anti-actin drugs, 62 cables, 138, 142 caps, 62 cortical patches, 142 cytoskeleton, 142 filasome, 37, 38 microfilaments, 258, 323 plaques, 62 actomyosin ring, 151 ade2, 51, 52, 57 adenylyl cyclase, 176 adhesins, 300 adhesion, 101, 178, 183, 219–225, 238, 253–257 affinity probes, 24 Alexa dyes, 53 alkaline phosphatase, 53, 60, 73 α-1,3-glucan, 99, 101, 102, 104, 105, 112 α-1,6-galactan, 106 α-factor, 71 α-tubulin, 62 AmCyan, 53, 56 amino acid permeases, 273 amino acid starvation, 171 amoeboid locomotion, 237 anaplerotic pathway, 301 anastomoses, 309, 311 anastomosis, 320, 321 aniline blue, 105 antibiotic macrolide, 68 antibody, 66 exopolyphosphatase, 66 AoVam3p, 51, 54 AP-3 adaptor protein, 73 AP-3 complex, 53 apical vesicles, 33, 52, 53, 258–262 appressoria, 37, 90, 228, 230, 238, 246, 253–270 ApsA, 127 APSES family, 177 arbuscular mycorrhiza, 291 ARF-GAP, 10, 24, 31, 41 ARF-GEF, 10, 21, 31, 32 arginine, 67 armadillo repeats, 54 Arp1, 63 Arp2/3, 151 ASH1, 143 atmA, 129 atomic force microscopy, 238, 241, 247 ATP, 67, 68 driven chaperone, 60 hydrolysis, 60, 68 synthase, 68 ATPase, 67 Mg2+ -ATPases, 75 plasma membrane H+ -ATPase, 68 V-ATPase, 67, 68 vacuolar H+ , 67 attachment, 219, 221, 254, 255, 264, 294 auto-signaling hypothesis, 227 autophagosome, 73 autophagy, 54 macroautophagy, 64, 73 auxins, 295 axl2, 147 bafilomycin, 68 Bary, Anton de, 242 BCECF, 67 Bem1, 140, 147, 148 Bem3, 146, 147 β-1,3-glucan, 98–103, 108, 183 β-1,4-glucan, 109 β-1,6-glucan, 98, 99, 103–105 Bim1, 143 biofilm, 183 biofilms and mating, 213 biotrophic, 26, 70, 269–275, 302 biotrophs, 252 Bni1, 131, 139, 150–152, 156 Bnr1, 150 BOI1, 157 BOI2, 157 branching factor, 295 brefeldin A, 30, 39 BODIPY, 54 bud, 57, 58, 63 clathrin-coated, 59 developing (in yeast), 50 bud site marker, 143 Bud3, 143 Bud4, 143 Bud10, 143 Bud1, 147 Bud2, 147, 157 334 Bud3, 147 Bud4, 147, 152 Bud5, 147 Bud6, 143, 150–152, 156 budding, 168 vacuole bounding membrane, 72 butyl methyl methacrylate embedment, 56 Ca localization, 67 Ca2+ , 51, 67, 225 Ca2+ gradient, 130 cables, 143 CAD1, 75 cadmium, 75 calcineurin, 183 calcium, 60 calcium channel, 183 calcium signaling, 183 calmodulin, 60, 183 cAMP, 257 cAMP pathway, 175 cAMP signaling, 171 capsule, 105 carbohydrate-active enzymes, 298 carboxy-DFFDA, 50–52, 54, 55, 68 carboxyfluorescein, 51, 67 carboxypeptidase Y, 54, 70 carboxySNAFL, 67 catabolic repression, 275 CCN1, 141 Cdc12, 152 Cdc2, 138 Cdc24, 138, 139, 146–149, 173 Cdc28, 138–141, 149 Cdc34, 142 Cdc42, 138, 139, 145–149, 151–153, 173 Cdc5, 142 CDCF, 67 CDF, 75 cell, 50, 52, 56, 59 animal, 52, 58, 70–72, 74 cycle, 51, 58 eukaryote, 50, 60, 72 expansion, 71 fixation, 56 fractions, 65 freeze-substituted, 72 guard, 58 hyphal, 62 hyphal tip, 49, 59, 74 live, 64 living, 49, 51, 53–55, 57, 66, 76 logarithmic, 67 mammalian, 73, 74 penultimate, 58, 67 periphery, 63 plant, 53, 73, 75 preservation, 56 stationary, 67 surface, 71 tip, 2, 26, 50, 57, 58, 67, 69 to cell, 69 wild-type, 53, 67, 74 Subject Index zinc-depleted, 74 cell cycle, 99, 169, 185 cell end makers, 129 cell polarity, 20, 127, 168, 185 cell tracker, 76 reagents, 51 cell wall, 52, 65, 72 cell wall biosynthesis, 185 cell wall construction genes AGS1, 109 Ags1p, 99 agsA, 112 Bgl2, 107, 110 CHS, 108, 109 Crh, 110 Dcw1, 111 Dfg5, 111 Ecm33, 110 FKS1, 106, 108 FKS2, 111 Gas, 110 Gel, 110 Hoc1, 108 Kre6, 104, 105, 109 MOK1, 109 MOK11, 109 MOK12, 109 MOK13, 109 MOK14, 109 Phr, 110 Sps2, 110 cell wall expansion, 238 cell wall extension, 245 cell wall integrity pathway, 111 cell wall morphology, 98–100 yeast walls, 105 cell wall polysaccharides α-1,3-glucan, 99, 101, 102, 104, 105, 112 α-1,6-galactan, 106 α-glucan, 101 β-1,3-glucan, 98, 102 β-1,4-glucan, 101, 109 β-1,6-glucan, 98, 99, 103–105 chitin, 98, 102, 105 galactomannan, 103 galactosaminogalactan, 103 glucuronoxylomannan, 105, 106 poly-N-acetylgalactosamine, 103 cell wall proteins Bad1, 107 Bad1p, 101 GPI-CWP, 98 PIR cell wall protein, 106 PIR proteins, 98 cell wall-degrading enzymes, 246, 274 cellular automata models, 321 cellular compartmentalization, biochemistry of, 24 cerato-platanin, 299 CFDA, 51, 52, 54, 70 chemical fixation, 49, 55, 56, 58, 65, 70 chemotaxis, 252 chitin, 100, 183 chitin synthase, 108, 183 Subject Index chloride channel, 30 chloromethyl dyes, 52, 76 Chs2, 143 Cla4, 150–152 clathrin, 2, 18, 31, 36, 38, 41, 56, 59, 72, 73 associated proteins, 17 binding proteins, 17, 36 light chain, 36 CLB2, 140 CLIP170, 126 ClipA, 126 Cln1, 139–141 Cln2, 139–141 Cln3, 139–141 CMAC, 51, 52, 54, 55, 76 CMFDA, 51, 52, 55, 76 CO2 , 170 cobalt, 74 COG complex, 11, 15, 17, 34, 36 comparative genomics, 22 concanamycin, 68 concanavalin A, 24, 25, 28, 39, 40, 56 confocal laser scanning microscopy, 11 conidia, 52, 53 conidiation, 228 conidiophores, 53 cord, 309, 316, 319, 325 cortical actin, 125 cortical markers, 138 cortical patches, 143 Cot1p, 74 Cph1, 173 CPY, 70, 73 pathway, 73 cryofixation, 56, 65, 66 cryosections, 59 Cvt pathway, 73 CWI pathway, 112 cyclin, 185 hypha-specific, 180 cyclophilin, 268 cyst germination, 256 cysteine protease, 179 cysts, 226 cytochalasin, 62, 130 cytodifferentiation, 294 cytoplasm, 64, 66–69, 73, 74, 76 tip, 58 to vacuole pathway, 73 cytoplasmic streaming, 50, 58, 70 cytoskeleton, 23, 26, 51, 56, 61–63, 70, 76, 123, 142, 244, 245, 276 vacuolar integrity, 26 diffusion, 64, 68–70, 74, 76 coefficient, 69 DiOC6 (3), 55 DLVO theory, 221 DNM1, 59 DSL1, 34 dynactin, 63 dynamin, 6, 17, 18, 37, 59, 61 related proteins, 18, 24, 37, 41 335 dynein, 62, 63, 127, 128 cytoplasmic, 63 EB1, 124 ectomycorrhiza, 299 ectomycorrhizal mantle, 293 ectomycorrhizal mutant, 302 Efg1, 175 EGFP, 51, 54 electron microscopy, transmission, 24 three-dimensional imaging, 24 electrotaxis, 252 embedding, 171 embedding pathway, 180 EMTOC, 124 encysted, 226 encysted zoospore, 229 encystment, 227 endocytic compartment early, 71 endocytic pathway, 52, 53, 56, 70–72 endocytosis, 2, 13, 16, 31, 36–38, 41, 52, 53, 59, 71, 72, 143, 148, 154, 261, 323 endomembrane, 56 endomembrane system, endoplasmic reticulum, 23, 24, 54, 55 cisternal sheets, 25 comparative genomics, COPII proteins, 8–11 ER-Golgi anterogade pathway, 8, 30, 31 ER-TrackerTM , 54 filamentous fungi vs yeast, 26 motility, 26 peripheral network, 25, 40 proteins, 3, luminal, membrane, smooth, 25 tubular–vesicular network, 26 endosomal pathway, 72 endosome, 11, 16, 36–39, 51–54, 61, 62 early, 52, 63, 70, 71 late, 19–21, 35, 38, 39, 54, 70, 71 membrane proteins, 21 prevacuolar, 70 prevacuolar compartment, 20 proteins, 19–22 recycling to Golgi, 20 sorting, 71 sorting complexes, 19 transport, 20 environmental stress, 170 enzyme, 53, 56, 60, 67, 68, 73 hydrolytic, 67 ER-TrackerTM , 19, 54 esterases cytoplasmic, 52 Exo70, 145, 146, 153 exocyst, 138, 145, 148, 153, 185 exocytosis, 22, 32, 53, 72, 153, 276 proteins, 19–22 extracellular matrix, 221, 255 extrahaustorial matrix, 271 extrahaustorial membrane, 271 336 Subject Index extramatrical mycelium, 293 Far1, 140, 142, 147, 149 farnesol, 183 filasome, 23, 28, 37, 38, 261, 262 fission yeast, 144 Fkh2, 141 flagella, 252 flow cytometry, 54 fluorescence recovery after photobleaching (FRAP), 49, 64, 68, 324 fluorescent probes, 49, 51, 54, 55, 57, 64, 67, 73, 76 dextrans, 52, 72 FuraZin-1, 74 LysoSensor, 51 LysoTracker, 51 membrane-impermeant, 52 fluorescent proteins, 2, 25, 26, 32, 41, 51, 53, 90, 123, 125 reef coral FP, 40, 53 FM1-43, 52, 53 FM4, 53 FM4-64, 51–55, 61, 71, 72, 156 For3, 129 foraging strategies, 310 freeze substitution, 24, 28, 33, 38–40, 49, 55–57, 65, 66, 70, 72, 73, 269 vacuolar diffusive, 69 freeze-dried, 65 freeze-drying, 66 frozen bulk specimens, 66 frozen section, 65, 66, 70 frozen-hydrated, 66 fruiting body, 292 functional complementation, 11 functional mycelial unit, 309 Fus3, 149 Fzo1, 59 Fzo1p, 59 G protein, 253 G protein complex, 149 G1 arrest and mating, 210 G1 cyclin, 139, 140 G2 cyclin, 139, 140 galactosamine, 104 galectins, 107 γ-tubulin, 124 GARP complex, 19 gene deletion, 7, 11 expansions, 41 targeting, 2, genetic mycelial unit, 309 genome, 297 germ tube, 50, 52, 70, 169, 253, 258 germination, 26, 224–230, 238, 257–260 GET complex, 31 GFP (green flourescent protein), 51, 53–56, 59–63, 73, 76 Gic1, 150, 152 Gic2, 150, 152 Gin4, 142–144 Glomeromycota, 291 glucose, 170 glutamine, 301 glutamine synthetase/glutamate synthase cycle, 302 glutathione, 51, 52, 75, 76 glycogen, 38, 259, 260, 266, 267 glycoproteins galactomannoproteins, 99, 100, 104 mannoproteins, 98 glyoxylate pathway, 299 Golgi, 1, 28–34, 53, 54, 57, 59, 62, 72, 107, 112, 139, 143, 145, 262 Golgi apparatus, 5, 24, 27, 41 concanavalin A binding sites, 28 COPI proteins, 8–11 fenestrated cisternae, 28 Golgi-ER retrogade pathway, 8, 9, 19, 30 matrix proteins, 29 proteins, 5–7, 29–32 resident, 5, retention, stacked membranes, lack of, 27, 29, 41 Golgi vesicles, 51 golgins, 6, 29 GORASPs, 6, 29 grazing, 319, 320 growth, 49, 58, 69 bipolar, 62 conditions, 66 form, 51 inhibiting conditions, 58 logarithmic, 67 medium, 54 microtubule, 54 rate, 52, 55 tip, 2, 41, 72, 142, 144, 155, 185, 227, 260, 262, 320, 322 GTP, 59, 60 GTPγS, 59 GTPase, 60, 61, 173 Hartig net, 72, 293 haustoria, 228, 269 haustoria expressed secreted proteins, 298 haustorial mother cells, 269 HDEL/KDEL receptors, 27, 41 hemibiotrophs, 252 heterokaryon incompatibility, 298 HEX-1, 89–92 alternative splicing, 90 crystal lattice, 91, 92 immuno-gold detection, 89 peroxisome targeting signal (PTS-1), 90 self-assembly, 90 hex-1, 93 mRNA transcripts, 93 phylogenetic distribution, 93 HGC1, 141 histone deacetylase, 177 Hof1, 151 homotypic vacuole fusion, 50, 52, 54, 59–61, 73 HOPS complex, 19 Hsl1, 142 hydrophobicity, 221, 254 hydrophobins, 264, 296 hydroxyurea, 142 hypaphorine, 295 hypha Subject Index anastomosis, 87 evolution, 87 mycelium, 87 hypha-to-yeast morphogenesis, 168 hyphae, 167 hyphal apex, 23, 33, 125, 130, 154, 155, 260, 261 hyphal development, 172 hyphal growth rate, 227 hyphal orientation, 184 hyphal tip cell, 2, 22, 23 hyphopodia, 228 hypoxia, 171 hypoxia pathway, 180 immunocytochemistry, 25, 38, 55, 56, 72, 266, 271, 272 immunofluorescence, 56, 60, 71 immunogold, 56, 59 immunolocalization, 62, 123, 273 inducible promoters, 22 infection strategies, 251 infection vesicle, 270 inositol phosphate signaling, 184 interfacial matrix, 272 invertase, 100, 272, 273 ion and phytochelatins, 75 distribution, 76 extraction, 74 redistribution, 65, 66 retaining, 55 sequestration in vacuoles, 74 toxic, 74 transport, 67 Iqg1, 152 isoamyl alcohol, 141 isotropic growth, 138 Kar9, 143 Kin1, 62 kin2, 53 kin3, 62, 63 kinesin, 62, 63, 127, 158 KipA, 126, 157, 158 L-systems, 322 lanthanum, 72, 224, 226, 229 latrunculin B, 62, 130, 144, 157, 258 lipid raft, 129 LMA1, 60 Lucifer Yellow, 52, 71 LY-CH, 52, 53, 55, 72 lysosomal compartment, 19, 38, 39 magnesium, 67 Mal3, 144 mannoproteins, 299 mannose-6-phosphate receptors, 38 mannosyl-phosphate, 108 MAP kinase, 257 MAPK pathway, 172 mass fractal dimension, 314 mastigonemes, 253 mathematical models, 320 mating Candida albicans, 195 Candida dubliniensis, 208 Candida glabrata, 198 mating on skin, 209 mating pheromone, 71, 149 mating type like (MTL) locus, 197 MDY-64, 51 mechosensitive Ca2+ channel, 230 melanin, 98, 106, 230, 246, 265 membrane cell, 49 channel, 68 domain, 56 dynamics, 56 endosomal, 73 flow, 55, 56 fusion, 50, 59, 60, 73 immobilization, 56 impermeant, 52 inner mitochondrial, 59 interaction, 55 internalisation, 71, 72 invagination, 61, 64, 73 label, 51, 53 outer mitochondrial, 59 permeant ester, 67 plasma, 52, 53, 59, 65, 71–74 potential, 51 recycling assay, 52 retrieval, 70, 72 scission, 59 selective dyes, 52 target, 60 targeting, 71 transfer, 70 transport, 76 vacuole, 50–54, 61, 67, 68, 71–74 vesicle, 60 membrane fusion, 36 metallothionein, 268, 273, 299 Mgm1p, 59 microelectrodes, 65 microscopy confocal, 49–51, 53, 56, 57, 61, 66 differential interference contrast (DIC), 49, 51, 55 electron, 49, 55–57, 59, 65, 70–72 fluorescence, 50, 57 light, 55 video, 51 microtubule, 63, 144, 258 and tubular vacuole network, 59 and vacuolar tubules, 62 depolymerisation, 62 drugs, anti-, 58, 62, 74 elongating, 62 gliding, 63 growth, 54 longitudinal, 62 motility, 63 motors, 54, 60, 62, 63 Ni2+ disruption, 74 tracks, 62, 63 microtubule cytoskeleton, 323 microtubule plus end, 125 337 338 Subject Index microtubules, 26, 37, 49 mitochondria, 53, 54, 59, 62, 143 fusion and fission, 58 inheritance, 59 microfilament, 63 movement, 63 movement of, 62 network, 74 positioning, 63 tubular, 54 tubular networks, 58, 59 mitochondrial, 56 outer membrane, 59 mitogen-activated protein (MAP) kinase pathway, 172 mitotic exit network, 143 Miyoshi, Manabu, 242 Mlc1, 139, 145, 152, 156, 159 Mn, 74 Mod5, 127, 129 morphogenetic checkpoint, 185 morphogenetic signaling pathway, 170 motility, 74 actin filament-based, 63 effects of zinc and nickel on, 74 endosome, 62 larger vacuoles, 74 organelle, 62 transport along the vacuolar conduit, 74 tubule, 76 vacuole, 49, 51, 55, 58, 61–63, 68, 69, 76 Msb3, 145, 150, 152 Msb4, 145, 150, 152 MTOC, 124 multiphoton microscopy, 11 multivesicular bodies, 38, 39, 56, 71–73 mutant class E vacuole protein sorting, 70 MVB, 71, 72 mycelial network, 49, 309 adjacency matrix, 311, 319 α−index, 313 alpha coefficient, 318 betweenness centrality, 315, 318 central point dependence, 318 central point dominance, 315, 317 clustering coefficient, 313, 318 control, 310 coordination, 326 cost, 310, 312, 314 cyclomatic number, 313 diameter, 314, 318 electrical circuit analogue, 319 global efficiency, 315, 319 graph theory, 311 hub and spoke models, 322 link weight, 313, 318, 319 meshedness coefficient, 318 node degree, 313, 316 node strength, 313, 317 reachability, 315, 317, 319 resilience, 310, 315, 317, 319 shortest path, 314, 317, 318 topology, 313 transport, 310, 314, 318, 319, 323 vulnerability, 315, 319 weighted, 311 mycelium, 88 peripheral growth zone, 88 mycorrhiza, 66, 69, 75, 291 arbuscular, 50, 70 ecto-, 49, 65, 67, 70, 72, 76 MYO1, 143 Myo2, 63, 139, 143, 145 MYO4, 143 myosin, 7, 29, 63, 109, 121, 130, 131, 143, 151, 183, 258 N-acetylglucosamine, 172 N-glycosylation, 107 nanogold internalisation of, 71 neckbands, 271 necrotrophs, 252 negative regulation, 181 NETO, 138 neutral red, 51 nickel, 74 nitrogen, 74 starvation, 73 storage of, 67 supply, to growing hyphal tips, 69 transport, 69 NKIN, 63 NMR, 65–67, 76 nocadazole, 142 nonconventional export, 107 NSF, 60 Num1, 127 nutrient, 58 micro-, 75 nutrient acquisition, 293 nutrient mobilisation, 276 nutrient transport, 70, 318, 323 bi-directional movement, 325 diffusion, 324 mass flow, 324, 325 non-invasive mapping, 325 phase domains, 326 pulsatile component to N-transport, 326 Nyv1p, 60 O-glycosylation, 107 oestrodiol, 171 Oomycetes, 251 phylogenetically, 251 optical tweezer, 241 Oregon Green, 51 organic nitrogen, 292 osmolality, 237, 238, 244 osmotic pressure, 237 osmotic stress, 244, 245 oxygen, 170, 300 PacC, 179 PAK kinase, 151 pathway diffusive, 69 vacuolar, 69 Pea1, 150 Subject Index penetration peg, 246, 253, 268 Pep12, 54, 71 peripheral growth zone, 311, 324 peroxisomes, 143 pH, 54, 71 ambient, 171 cytoplasmic, 67 intracellular, 51 vacuolar, 73 vacuole, 49, 67 pH signaling, 171 pH signaling pathway, 178 pheromone, 209–212 pheromone response pathway, 173 phosphate, 67, 69, 74 phosphodiesterases, 177 phospholipase, 300 phospholipase C, 184 phosphorus, 66, 67, 74, 301 photon-counting scintillation imaging, 325 Pkc1, 146 plasma membrane, 36 PO3− , 74 Poiseuille equation, 311 polarisome, 130, 138, 150, 158–160, 185 polarity, 262 polarized growth, 168 polarized secretion, 145 polyphosphate, 64–67, 73, 76, 301 Pom1, 144 potassium, 66, 67, 74 prenyl residue, 129 pressure probe, 239, 241 prevacuolar compartment, 11, 20, 54, 70, 73 primary septum, 143 probenecid, 52 progesterone, 171 protease, 60, 243, 298 protein kinase A (PKA), 177 protein kinases, 174 protein(s) basic, 67 endomembrane, 3–22 glycosylation, 33 localisation, 60 motor, 63 multidrug resistance-associated, 75 retrieval, 72 secretion, 32 sorting, 67, 70, 71, 76 sorting pathway, 54 targeting, 49, 61, 67, 70, 71 transport, turnover, 72 vacuole fusion, 54 proteolytic processing, 67 proteomic, 253 protoplast, 71 pseudohypha, 167 pulsatile growth, 242 punctate structures, 52, 54 PVE, 70 Q-SNAREs, 12, 60 quantitative trait locus, 302 quinacrine, 51 quorum-sensing, 182 R-SNAREs, 12, 60 Rab, 59–61 RAB BAPs, 13 RAB GAPs, 12–16, 34 RAB GEFs, 12–16, 34, 35 RAB GTPase, 12–16, 33, 34, 41, 145 Rac, 131 Rac GTPase, 146 CflB, 146 Rac1, 146 Ras1, 176 ratio, 61 -metric analysis, 54, 74 imaging, 67 RCY1, 71 rcy1, 71 Rdi1, 147 receptors, 294 repression, 181 Rga, 146, 147, 153 rhizomorphs, 247, 293, 302 Rho, 131 Rho1, 146, 150, 151, 153 RHO3, 157 Rho3, 145, 153 Rho4, 146, 151 rhodamine 123, 54 Rhodamine B, 54 Rsr1, 147, 148, 157 SAR1 GTPase, 9, 32 Sec2, 145 Sec3, 145 Sec4, 145, 146, 152 Sec9, 146 Sec12, 32 Sec15, 145, 153 Sec17p, 60 Sec18p, 60 secreted enzymes, 237, 243, 247 secretory pathway, 24, 32–36 secretory vesicles, 137, 139, 143, 145, 153 segregation structure, 50, 57, 58, 63, 70 SepA, 131, 156 septa, 50, 87, 98, 138, 143, 168 septal pore cap, 25, 26, 40, 87 septins, 143, 153, 169, 183 Cdc10, 143 Cdc11, 143 Cdc12, 143 Cdc3, 143 Shs1, 143 septum, 50 serum, 170 shmoos, 138, 144 Sic1, 139, 140 signal transduction, 257 signals, 294 Slt2, 150 SNAP, 60 339 340 Subject Index SNARE, 12–16, 33, 34, 53, 59–61 complex, 60, 73 mediators, 12 regulators, 60 SNARF, 67 Snc1, 53 SOL1, 142 SPA2, 137 Spa2, 150–152, 156 SpaA, 131, 156, 157 spindle pole body, 122, 124 Spitzenkörper, 2, 52, 53, 89, 100, 121, 139, 153, 158–160, 185, 228, 260 spore, 252 dormancy, 257 germination, 256, 259 spore tip mucilage, 221, 254 START, 185 Start, 139 Ste11, 152 Ste2, 71, 149 Ste20, 150–152 Ste20/p65PAK family, 174 Ste3, 149 sterol biosynthesis, 27 stomata, 262, 265 strain gauge, 239–243, 245 stretch-activated channel, 171, 183, 227 strigolactones, 295 structure cellular, 56 styryl dyes, 51 sugar transporter, 273 surface topographical feature, 230 Swe, 141 switching and mating competence, 203 swoD, 131 swoF, 131 symbioses, 292 synteny, 297 t-SNARE, 51, 54, 59–61, 71, 145 Sec9, 145 Sso1, 145 Sso2, 145 Tea1, 127, 129, 144, 157 Tea2, 126, 138, 144, 157 Tem1, 143 temperature, 170 tetraspanin, 268 thermal dimorphism, 101 thigmotropism, 262 tip growth, 144, 155, 260, 320 tip high Ca2+ gradient, 225, 227 Tip1, 126, 144 tissue-degrading enzymes, 242 Tlg1p, 71 Tlg2p, 71 tomography, electron, 24 tonoplast, 52 topography, 263 Tpk isoform, 177 transcript profiling, 182 transcription factor, 173, 253 transcriptome, 298 transformation, 303 transport basic amino acids, 67 diffusive, 69, 73 endosome, 63, 72 glutathione-conjugate, 75 long-distance, 49 longitudinal, 64, 68 microtubules, 63 nitrogen, 67, 68, 76 nutrient, 50, 74–76, 309 organelle, 60, 62 organic anion, 52 phosphate, 67–69, 76 phytochelatin-Cd complex, 75 protein, 69, 72 proton, 68 rate, 69 retrograde, 61 sugar, 69, 70 tubule, 57, 61, 68, 69, 76 vacuole, 49, 64, 65, 68–70, 74–76 vacuole content, 57 vesicle, 57, 60, 69 zinc, 75 transporter, 71, 300 ABC, 75 ATP-binding cassette, 75 cation, 74 CDF, 74 efflux, 74, 75 glutathione, 52 influx, 74 sugar, 274 vacuole membrane, 74 zink, 74 transposable elements, 297 TRAPP complex, 8, 26 trimeric G protein, 138 tubule, 50, 53–59, 61, 64, 68, 69, 72–74, 76 tubulin, 74 Tup1-Ssn6 corepressor, 181 turgor pressure, 238, 260 tyresol, 183 ubiquitin, 178 ubiquitination, 71 ugo, 59 Ugo1p, 59 ultrastructure, 55, 56, 72, 76 urea, 302 v-SNARE, 60, 145 Snc1, 145 Vac8, 54 Vac8p, 61 vacuole(s), 11, 19, 38, 49–76, 143 acidification, 67, 68, 74 amino acids in, 67 detoxifying, 49, 74–76 differentation, 49 differentiation, 51, 55, 68, 73, 75 motile, 49–76 Subject Index protein, 19–22 solute transport, 324 spherical, 49, 50, 54, 55, 61, 62, 69, 73, 74 system, 323 transport, 51 tubular, 49–76 Vam3, 54 Vam3p, 54, 59, 60, 71, 73 Vam7p, 61 vesicle(s), 53, 55–59, 62, 63, 65, 71–73, 76 apical, 52, 53 coated, 51, 59, 72 COPI, 8–11, 30 COPII, 8–11, 30 docking, 60 fusion, 60, 61, 69 movement, 323 supply centre, 122, 261 targeting, 73 trafficking, 31, 33, 56 virulence factor, 168 Vph1p, 61 VPS pathway, 73 vps, 70, 71 Vps1, 59 VSC, 122 wall degrading enzymes, 269 Wee1, 141 white–opaque switching, 201 whole-genome duplication event, 24, 27 whole-genome shotgun, 297 wood wide web, 309 Woronin body as adaptation, 93 function, 90 genesis, 91 inheritance, 93 purification, 89 turgor pressure, 91 ultrastructure, 88 X-ray microanalysis, 65, 66, 74 yeast, 50–54, 56, 57, 59–61, 63–65, 67, 70–76 yeast–hypha morphogenesis, 171 Yeb3, 54 Ypt31, 145 Ypt32, 145 Ypt7, 59–61 Yup1, 61 zinc, 74, 75 zinc shock, 74, 75 -depleted cell, 74 zoospores, 252 motility, 253 zoosporogenesis, 229 Zrc1p, 74 Zrt3p, 74, 75 341 ... copyright All rights are reserved, whether the whole or part of the material is concerned, specifically the rights of translation, reprinting, reuse of illustrations, recitation, broadcasting, reproduction... Vöckler GbR, Leipzig, Germany Printed on acid-free paper SPIN 11313472 31/3180 543210 Karl Esser (born 1924) is retired Professor of General Botany and Director of the Botanical Garden at the Ruhr-Universität... of Applied Microbiology, Hertzstrasse 16, D-76187 Karlsruhe, Germany XX List of Contributors M Fricker (e-mail: mark.fricker@plants.ox.ac.uk) Department of Plant Sciences, University of Oxford,