Hoffmeister Biochemistry and Molecular Biology

3rd Auflage 2016
ISBN: 978-3-319-27790-5
Verlag: Springer Nature Switzerland
Format: PDF
Kopierschutz: 1 - PDF Watermark

E-Book, Englisch, Band 3, 403 Seiten

Reihe: The Mycota

This new edition provides a comprehensive look at the molecular genetics and biochemical basis of fungal biology, covering important model organisms such as Aspergilli while also integrating advances made with zygomycetes and basidiomycetes.
This book groups a total of 15 chapters authored by expert scholars in their respective fields into four sections. Five chapters cover various aspects of gene expression regulation. These range from regulation in organismal interactions between parasitic fungi and their host plant, heavy metal stress and global control of natural product genes to conidiation and regulation through RNA interference. Two chapters are dedicated to signal transduction, highlighting MAP-kinase-dependent signaling and heterotrimeric G-proteins. Fungal carbohydrates are the subject of the third section, which addresses both polymeric cell wall carbohydrates and trehalose as an important, low molecular weight carbohydrate. The fourth section emphasizes the metabolism of major elements (carbon, nitrogen, sulfur) and critical cellular pathways for primary and secondary products.


Professor Dr. Dirk Hoffmeister
Friedrich-Schiller-Universität, Pharmazeutische Mikrobiologie, Jena, Germany

Autoren/Hrsg.

Hoffmeister, Dirk

Inhaltsverzeichnis

1;Series Preface;8
2;Volume Preface;12
3;Contents;14
4;List of Contributors;16
5;Regulation of Gene Expression;20
5.1;1 Molecular Biology of Asexual Sporulation in Filamentous Fungi;21
5.1.1;I. Introduction;21
5.1.2;II. Asexual Sporulation in Aspergillus nidulans;21
5.1.2.1;A. Morphology of Asexual Structure;21
5.1.2.2;B. Regulators of Asexual Development;22
5.1.2.2.1;1. Central Regulators of Conidiation;22
5.1.2.2.1.1;a) BrlA;22
5.1.2.2.1.2;b) AbaA;23
5.1.2.2.1.3;c) WetA;23
5.1.2.2.1.4;d) StuA and MedA;23
5.1.2.2.2;2. Controllers of the Central Regulators;24
5.1.2.2.2.1;a) FluG-Mediated Signaling Pathway;24
5.1.2.2.2.2;b) Heterotrimeric G Protein Signaling Pathways;25
5.1.2.2.2.3;c) MAP Kinase Signaling Pathways;26
5.1.2.2.2.4;d) The Velvet Family Proteins;26
5.1.2.2.2.5;e) Light and Signals;27
5.1.2.2.2.6;f) Developmental Balancers;27
5.1.2.2.2.7;g) Other Transcription Factors;28
5.1.2.2.3;3. Feedback Regulators of Conidiation;28
5.1.3;III. Asexual Sporulation in Penicillum marneffei;28
5.1.3.1;A. Morphology of Asexual Structure;28
5.1.3.2;B. Regulators of Asexual Development;30
5.1.4;IV. Asexual Sporulation in Fusarium graminearum;30
5.1.4.1;A. Morphology of Asexual Structure;30
5.1.4.2;B. Regulators of Asexual Development;31
5.1.5;V. Conclusions;32
5.1.6;References;33
5.2;2 Insight into Fungal Secondary Metabolism from Ten Years of LaeA Research;38
5.2.1;I. Introduction;38
5.2.2;II. LaeA Mechanism;39
5.2.2.1;A. Methyltransferase;39
5.2.2.2;B. Epigenetics;39
5.2.2.3;C. Velvet Complex Member;39
5.2.3;III. Secondary Metabolites Regulated by LaeA;40
5.2.3.1;A. Aspergillus species;40
5.2.3.2;B. Other Genera;40
5.2.4;IV. Processes Identified Through LaeA Microarrays;42
5.2.5;V. Processes Identified Through LaeA Mutagenesis;42
5.2.6;VI. Conclusion;43
5.2.7;References;43
5.3;3 RNAi Function and Diversity in Fungi;47
5.3.1;I. Introduction;47
5.3.1.1;A. Evolution of RNAi and Its Protein Components;48
5.3.2;II. RNAi Function;49
5.3.2.1;A. Quelling;50
5.3.2.2;B. Meiotic Silencing by Unpaired DNA;52
5.3.2.3;C. Heterochromatin Formation and Transcriptional Gene Silencing;53
5.3.2.4;D. Sex-Induced Silencing;55
5.3.3;III. MicroRNAs;55
5.3.4;IV. RNAi During Plant-Microbe Interaction;56
5.3.5;V. RNAi as a Biotechnology Tool;57
5.3.6;VI. Conclusion;58
5.3.7;References;58
5.4;4 Fungal Molecular Response to Heavy Metal Stress;62
5.4.1;I. Introduction;63
5.4.2;II. Thou Shall Not Pass!: Extracellular Response upon Metal Toxicity;65
5.4.2.1;A. Metal Sorption to the Cell Wall;65
5.4.2.2;B. Release of Metal-Binding Substances;67
5.4.2.2.1;1. Interaction of Organic Acids with Metals;67
5.4.2.2.2;2. Oxalic Acid;68
5.4.2.2.3;3. Further Organic Acids;68
5.4.2.2.4;4. Siderophores;69
5.4.2.2.5;5. Glutathione;69
5.4.3;III. Leave Someone Holding the Baby: Intracellular Processes and Transport;69
5.4.3.1;A. Regulation of Metal Influx;69
5.4.3.2;B. Metal Efflux Systems;71
5.4.3.3;C. Chelation and Chelate Transport;72
5.4.4;IV. System Reset: Alleviating Metal-Induced Damage;73
5.4.5;V. Perspective;74
5.4.6;References;75
5.5;5 Control of Gene Expression in Phytopathogenic Ascomycetes During Early Invasion of Plant Tissue;84
5.5.1;I. Introduction;84
5.5.1.1;A. Fungal Lifestyles;84
5.5.1.2;B. Comparative Genomics;84
5.5.1.3;C. Stages of Infection;85
5.5.2;II. Surface Recognition and Breaking Dormancy;88
5.5.2.1;A. Surface Recognition;88
5.5.2.2;B. Adhesion;89
5.5.2.3;C. Germination;91
5.5.3;III. Entry into the Plant;92
5.5.3.1;A. Direct Entry;93
5.5.3.1.1;1. Infection Structure-Initiated Entry;93
5.5.3.1.1.1;a) Developing Appressoria in Magnaporthe oryzae;93
5.5.3.1.1.2;b) Gene and Protein Expression in Mature Appressoria;94
5.5.3.1.1.2.1;i. Magnaporthe oryzae;94
5.5.3.1.1.2.2;ii. Colletotrichum Species;94
5.5.3.1.1.2.3;iii. Blumeria graminis;95
5.5.3.1.1.2.4;iv. Botrytis cinerea;96
5.5.3.1.1.2.5;v. Sclerotinia sclerotiorum;96
5.5.3.1.1.2.6;vi. Parastagonospora nodorum;97
5.5.3.2;B. Entry Through Stomata or Wounds;98
5.5.3.2.1;1. Gene Expression During Early Infection;99
5.5.3.2.1.1;a) Zymoseptoria tritici;99
5.5.3.2.1.2;b) Fusarium graminearum;100
5.5.3.2.1.3;c) Leptosphaeria maculans;100
5.5.3.2.1.4;d) Cladosporium fulvum;101
5.5.4;IV. Conclusions;102
5.5.5;References;102
6;Signal Transduction;110
6.1;6 Fungal MAP-Kinase-Mediated Regulatory Pathways;111
6.1.1;I. Introduction;111
6.1.2;II. The Pheromone Response and Filamentation MAPK Pathways;112
6.1.2.1;A. Saccharomyces cerevisiae;112
6.1.2.1.1;1. Pheromone Response in S. cerevisiae;112
6.1.2.1.2;2. Filamentous Growth of S. cerevisiae;114
6.1.2.2;B. Candida albicans;115
6.1.2.3;C. Filamentous Fungi;115
6.1.2.3.1;1. Aspergillus nidulans and Aspergillus fumigatus;115
6.1.2.3.2;2. Neurospora crassa;118
6.1.2.3.3;3. Cryptococcus neoformans;118
6.1.2.3.4;4. Plant Pathogenic Fungi;119
6.1.3;III. The Stress Response MAPK Pathway;119
6.1.3.1;A. Saccharomyces cerevisiae;120
6.1.3.2;B. Candida albicans;120
6.1.3.3;C. Filamentous Fungi;121
6.1.3.3.1;1. Aspergillus nidulans and Aspergillus fumigatus;121
6.1.3.3.2;2. Neurospora crassa;121
6.1.3.3.3;3. Cryptococcus neoformans;121
6.1.3.3.4;4. Plant Pathogenic Fungi;122
6.1.4;IV. The Cell Wall Integrity (CWI) Pathway;122
6.1.4.1;A. Saccharomyces cerevisiae;122
6.1.4.2;B. Candida albicans;123
6.1.4.3;C. Filamentous Fungi;123
6.1.4.3.1;1. Aspergillus nidulans and Aspergillus fumigatus;123
6.1.4.3.2;2. Neurospora crassa;124
6.1.4.3.3;3. Cryptococcus neoformans;124
6.1.4.3.4;4. Plant Pathogenic Fungi;124
6.1.5;V. Spore Morphogenesis in Saccharomyces cerevisiae;125
6.1.6;VI. Conclusions;125
6.1.7;References;126
6.2;7 Heterotrimeric G Proteins;132
6.2.1;I. Introduction;132
6.2.2;II. Components of Heterotrimeric G Protein Signaling;133
6.2.2.1;A. G?, Gbeta, and Ggamma Proteins;133
6.2.2.2;B. Guanine Nucleotide Exchange Factors (GEFs);136
6.2.2.2.1;1. G Protein-Coupled Receptors (GPCRs);136
6.2.2.2.2;2. Non-receptor GEFs;136
6.2.2.3;C. Regulator of G Protein Signaling (RGS) Proteins;138
6.2.2.4;D. Effector Pathways;138
6.2.2.4.1;1. cAMP-Dependent Protein Kinase (PKA);138
6.2.2.4.2;2. Mitogen-Activated Protein Kinase (MAPK);139
6.2.3;IV. Cellular Functions of G Protein Signaling Components in Yeast and Filamentous Fungi;140
6.2.3.1;A. Nutrient Sensing;140
6.2.3.1.1;1. Glucose Sensing in Saccharomyces cerevisiae and Schizoaccharomyces pombe;140
6.2.3.1.2;2. Carbon-Sensing Pathways in Neurospora crassa and Aspergillus nidulans;141
6.2.3.1.3;3. Methionine and Glucose Sensing in Cryptococcus neoformans;141
6.2.3.2;B. Mating and Pheromone Response;142
6.2.3.2.1;1. Ste2p/?-Factor and Ste3p/a-Factor in S. cerevisiae;142
6.2.3.2.2;2. Map3/M-Factor and Mam2/P-Factor in S. pombe;142
6.2.3.2.3;3. PRE-1/MFA-2 and PRE-2/CCG-4 in N. crassa;143
6.2.3.2.4;4. Mating and Cleistothecia Formation in Aspergillus;143
6.2.3.2.5;5. Mating in Cryptococcus neoformans;144
6.2.3.3;C. Pathogenesis and Virulence;144
6.2.3.3.1;1. Appressorium Formation and Pathogenicity in Magnaporthe oryzae;144
6.2.3.3.2;2. Pathogenesis in Ustilago maydis;146
6.2.3.3.3;3. Melanin and Capsule Formation in Cryptococcus neoformans;147
6.2.3.3.4;4. Quorum Sensing in Aspergillus;147
6.2.4;IV. Conclusions;148
6.2.5;References;148
7;Molecular Biology and Biochemistry of Fungal Carbohydrates;158
7.1;8 The Cell Wall Polysaccharides of Aspergillus fumigatus;159
7.1.1;I. Introduction;159
7.1.2;II. The Cell Wall of Aspergillus fumigatus Hyphae;160
7.1.3;III. Synthesis and Function of Cell Wall Polysaccharides;161
7.1.3.1;A. beta-1,3-glucan;161
7.1.3.2;B. Chitin;163
7.1.3.3;C. Galactomannan;163
7.1.3.4;D. ?-1,3-glucan;164
7.1.3.5;E. Galactosaminogalactan;165
7.1.4;IV. Modifications of Cell Wall Polysaccharides;165
7.1.4.1;A. Modification of beta-1,3-glucans;165
7.1.4.1.1;1. Endo-beta-1,3-glucanase (ENG Proteins);166
7.1.4.1.2;2. beta-glucanosyltransferase (GEL Proteins);166
7.1.4.1.3;3. Branching Enzymes, BGT Proteins;166
7.1.4.1.4;4. Other beta-1,3-glucan-Modifying Enzymes (EXO and SUN Proteins);167
7.1.4.2;B. Modification of Chitin;167
7.1.4.2.1;1. Chitinase, CHI Proteins;167
7.1.4.2.2;2. Chitin Deacetylase, CDA Proteins;167
7.1.4.2.3;3. Chitosanase, CSN Proteins;168
7.1.4.3;C. Modification of Other Cell Wall Polysaccharides;168
7.1.5;V. Towards an Understanding of the Regulation of Cell Wall Biosynthesis;169
7.1.5.1;A. Chemogenetic Approaches to Understanding the Regulation of Cell Wall Biosynthesis;169
7.1.5.2;B. Deciphering the Regulation of Cell Wall Composition Through Direct Molecular Approaches;170
7.1.5.2.1;1. Global Regulators of Cell Wall Biosynthesis;170
7.1.5.2.2;2. Other Compensatory Relationships Between Cell Wall Polysaccharides;171
7.1.5.3;C. Real World Applications: Targeting Compensatory Changes in Cell Wall Composition to Enhance Antifungal Efficacy;172
7.1.6;VI. Conclusions and Perspectives;172
7.1.7;References;172
7.2;9 Chitin Synthesis and Fungal Cell Morphogenesis;178
7.2.1;I. Introduction;178
7.2.2;II. Chitin Synthases and Deposition of Chitin at the Fungal Cell Wall;179
7.2.3;III. Chitin Synthases;180
7.2.3.1;A. The Diversity of Fungal Chitin Synthases: A Common Catalytic Centre for Multiple Functions;180
7.2.3.2;B. The Ancient Evolutionary Origin of Chitin Synthases;182
7.2.4;IV. Chitin Synthesis and Fungal Cell Wall Assembly;183
7.2.4.1;A. Chitin Synthesis and Cell Wall Assembly;183
7.2.4.2;B. Chitin Degradation and Cell Wall Assembly;185
7.2.4.3;C. Chitin Synthesis in Response to Cell Stress;185
7.2.5;V. A Single Polymer but Distinct Functions for Chitin Synthase Enzymes;185
7.2.5.1;A. The Biological Function of Family I CSs;185
7.2.5.1.1;1. Chitin Synthase I;186
7.2.5.1.2;2. Chitin Synthase II;186
7.2.5.1.3;3. Other Class I, II and III Fungal CSs;186
7.2.5.2;B. The Biological Function of Family II CSs;187
7.2.5.2.1;1. Chitin Synthase III (Class IV);187
7.2.5.2.2;2. Chitin Synthases with Myosin Motor-Like Domain;187
7.2.5.3;C. The Elusive Function of Class VI CSs;188
7.2.6;VI. Regulation of Chitin Synthases;188
7.2.6.1;A. Regulation of Family I CSs;189
7.2.6.1.1;1. Regulation of Chitin Synthase I;189
7.2.6.1.2;2. Regulation of Chitin Synthase II;189
7.2.6.1.3;3. Regulation of Other Class I, II and III Fungal CSs;191
7.2.6.2;B. Regulation of Family II CSs;192
7.2.6.2.1;1. Regulation of Chitin Synthase III;192
7.2.6.2.2;2. Regulation of Fungal Chitin Synthases During Mycelial Growth: Chitin Synthases with a Myosin Motor-Like Domain;194
7.2.7;VII. Chitin Synthesis and Antifungal Therapies;195
7.2.8;VIII. Concluding Remarks;196
7.2.9;References;196
7.3;10 Trehalose Metabolism: Enzymatic Pathways and Physiological Functions;202
7.3.1;I. Introduction;203
7.3.2;II. Occurrence of Trehalose;204
7.3.3;III. Biosynthetic Pathways for Trehalose;206
7.3.3.1;A. Trehalose-6-Phosphate Synthase and Phosphatase;207
7.3.3.2;B. Trehalose Phosphorylase;211
7.3.4;IV. Enzymes of Trehalose Hydrolysis: Trehalases;212
7.3.5;V. Functions of Trehalose;215
7.3.5.1;A. Trehalose as Storage Carbohydrate;215
7.3.5.2;B. Trehalose as Stress Protectant;217
7.3.5.2.1;1. Trehalose as Stress Protectant In Vitro;217
7.3.5.2.2;2. Trehalose as Stress Protectant In Vivo;218
7.3.5.2.3;3. Trehalose and Thermotolerance;220
7.3.5.2.4;4. Trehalose and Freeze Tolerance;221
7.3.5.2.5;5. Trehalose and Osmo- and Dehydration Tolerance;222
7.3.5.2.6;6. Trehalose and Other Stress Conditions;223
7.3.5.2.7;7. Other Stress Protectants;225
7.3.5.3;C. Trehalose as Carbon Source;226
7.3.5.3.1;1. Transport of Trehalose;226
7.3.5.4;D. Other Functions of Trehalose;228
7.3.6;VI. Regulation of Trehalose Metabolism;229
7.3.6.1;A. Cellular Signaling Pathways Controlling Trehalose Metabolism;229
7.3.6.1.1;1. Glucose-Induced Trehalose Mobilization: cAMP as Second Messenger;229
7.3.6.1.2;2. Fermentable-Growth-Medium-Induced Trehalose Mobilization: Nutrient Sensing by Transceptors;232
7.3.6.1.2.1;a) Nitrogen-Induced Trehalose Mobilization;233
7.3.6.1.2.2;b) Phosphate-Induced Trehalose Mobilization;234
7.3.6.1.2.3;c) Sulfate-Induced Trehalose Mobilization;235
7.3.6.1.2.4;d) Induction of Trehalose Mobilization by Other Nutrients;235
7.3.6.2;B. Posttranslational and Transcriptional Control of Trehalose Biosynthesis and Degradation;236
7.3.6.2.1;1. Posttranslational Regulation of Trehalose Biosynthesis;236
7.3.6.2.2;2. Posttranslational Regulation of Trehalose Degradation;238
7.3.6.2.3;3. Transcriptional Regulation of Trehalose Biosynthesis and Degradation;240
7.3.6.2.4;4. Trehalose Accumulation During Sublethal Heat Treatment;242
7.3.7;VII. Regulatory Functions of Trehalose Metabolism;246
7.3.7.1;A. Control of Growth, Cell Cycle Progression, and Sporulation;246
7.3.7.2;B. Control of Glycolysis by Tre6P;248
7.3.7.3;C. Yeast as a Model for Plant Trehalose Metabolism;254
7.3.8;VIII. Trehalose Metabolism as a Target for Antifungal Compounds;255
7.3.9;IX. Conclusions and Perspectives;260
7.3.10;References;260
8;Molecular Aspects of Biochemical Pathways;289
8.1;11 Regulation of Fungal Nitrogen Metabolism;290
8.1.1;I. Introduction;290
8.1.2;II. Regulation by Global and Pathway-Specific Transcription Factors;291
8.1.3;III. Global Regulation of Nitrogen Utilization Genes;292
8.1.3.1;A. Transcriptional Controls: The Key Players;292
8.1.3.1.1;1. The GATA Transcription Factor AreA;292
8.1.3.1.1.1;a) AreA Function;292
8.1.3.1.1.2;b) Conservation of AreA Function;293
8.1.3.1.1.3;c) Regulation of AreA Action;294
8.1.3.1.1.4;d) Regulation of areA mRNA Stability via Caf1, CutA, and RrmA;294
8.1.3.1.1.5;e) Regulation of AreA Subcellular Localization;294
8.1.3.1.1.6;f) Nitrogen Regulation via TOR Signaling;297
8.1.3.1.1.7;g) Unconventional Modes of AreA Action;297
8.1.3.1.2;2. The Corepressor NmrA;298
8.1.3.1.2.1;a) NmrA Function;298
8.1.3.1.2.2;b) Conservation of NmrA;299
8.1.3.1.2.3;c) Regulation of NmrA Function;299
8.1.3.1.3;3. The bZIP Transcription Factor MeaB;300
8.1.3.1.3.1;a) MeaB as a DNA-Binding Protein;300
8.1.3.1.3.2;b) Conservation of MeaB;301
8.1.3.1.3.3;c) Regulation of MeaB;301
8.1.3.1.4;4. AreB: A Second GATA Transcription Factor;302
8.1.3.1.4.1;a) AreB Is a Transcription Repressor of Nitrogen Metabolic Genes;302
8.1.3.1.4.2;b) Conservation of AreB;303
8.1.3.1.5;5. The Dual-Function Transcription Factor TamA;304
8.1.3.1.5.1;a) TamA Is a Coactivator of AreA;304
8.1.3.1.5.2;b) TamA Acts as a DNA-Binding Activator or as a Coactivator Depending on Promoter Context;304
8.1.3.1.5.3;c) Conservation of TamA;306
8.1.3.2;B. Posttranscriptional Controls;306
8.1.4;IV. Conclusions;306
8.1.5;References;307
8.2;12 Regulation of Sulfur Metabolism in Filamentous Fungi;313
8.2.1;I. Introduction;313
8.2.2;II. Acquisition of Sulfur;314
8.2.2.1;A. Sulfur Sources;314
8.2.2.2;B. Response to Sulfur Limitation;315
8.2.3;III. Detection of Sulfur Status;317
8.2.4;IV. Neurospora crassa Sulfur Regulatory System;319
8.2.4.1;A. CYS3 Regulator;319
8.2.4.2;B. Sulfur Controller Regulators;321
8.2.4.3;C. Operation of the Control System;322
8.2.5;V. Regulatory Comparison to Aspergillus nidulans and Saccharomyces cerevisiae;323
8.2.6;VI. Conclusions;324
8.2.7;References;325
8.3;13 The Regulation of Carbon Metabolism in Filamentous Fungi;328
8.3.1;I. Introduction;328
8.3.2;II. Glucose Transport and Sensing;329
8.3.3;III. Induction and Repression;330
8.3.4;IV. Carbon Catabolite Repression;331
8.3.4.1;A. CreA;331
8.3.4.1.1;1. A. nidulans creA Mutations;331
8.3.4.1.2;2. CreA Mutant Phenotypes in Other Fungi;332
8.3.4.1.3;3. Molecular Analysis of CreA in A. nidulans;332
8.3.4.1.4;4. Functional Analysis of CreA;334
8.3.4.1.5;5. Comparison Between Yeast and A. nidulans, and Within Filamentous Fungi;334
8.3.4.2;B. A Role for Regulatory Ubiquitination;337
8.3.4.2.1;1. A Role for Deubiquitination?;337
8.3.4.2.2;2. A Role for Ubiquitination?;339
8.3.5;V. Genome-Wide Studies;340
8.3.6;VI. Concluding Remarks;341
8.3.7;References;342
8.4;14 Special Aspects of Fungal Catabolic and Anabolic Pathways;348
8.4.1;I. Introduction;348
8.4.2;II. Propionyl-CoA, A Common Metabolic Intermediate;349
8.4.2.1;A. Degradation of Propionyl-CoA via the Methylcitrate Cycle;351
8.4.2.2;B. Alternative Propionyl-CoA Degradation Pathways in Fungi;352
8.4.3;III. Growth on Gluconeogenic Substrates;355
8.4.3.1;A. Utilisation of the Glyoxylate Cycle in Ascomycetes;355
8.4.4;IV. Amino Acid Biosynthesis and Utilisation as Nutrient Sources;357
8.4.4.1;A. Histidine Degradation in Fungi;358
8.4.4.2;B. Synthesis of the Amino Acid Lysine;360
8.4.5;V. Conclusions;363
8.4.6;References;363
8.5;15 Genetic and Metabolic Aspects of Primary and Secondary Metabolism of the Zygomycetes;368
8.5.1;I. Introduction;368
8.5.1.1;A. Zygomycetes: Evolution, Systematics, and Ecology;369
8.5.1.2;B. The Cooperative Nature of Zygomycetes: Bacterial-Fungal Alliances;370
8.5.2;II. Key Aspects in the Metabolism of Zygomycetes: Biotechnological Implications;371
8.5.2.1;A. Carotene Biosynthesis and Degradation: Primary Meets Secondary Metabolism;372
8.5.2.1.1;1. Regulation, Genetic Manipulation: What Have We Learned from the Major Model Organisms Mucor circinelloides, Phycomyces blak...;374
8.5.2.1.2;2. Carotene Degradation Is Linked to Sexual Interactions;377
8.5.2.2;B. Fatty Acids;379
8.5.2.3;C. Organic Acids;379
8.5.2.4;D. Storage Lipids and Single Cell Oils;380
8.5.2.5;E. Enzymes;381
8.5.3;III. The Dogma of the Unability of Zygomycetes to Produce Natural Products;382
8.5.4;IV. Conclusions;384
8.5.5;References;384
9;Biosystematic Index;393
10;Subject Index;397