Note: Förderkennzeichen BMBF 16GW0104K , Verbundnummer 01159901 , Paralleltitel dem englischen Berichtsblatt entnommen , Unterschiede zwischen dem gedruckten Dokument und der elektronischen Ressource können nicht ausgeschlossen werden , Sprache der Zusammenfassung: Deutsch, Englisch

Note: Förderkennzeichen BMBF 16GW0094K. - Verbund-Nummer 01157006 , Literaturverzeichnis: Seite 18-21 , Paralleltitel dem englischen Berichtsblatt entnommen , Unterschiede zwischen dem gedruckten Dokument und der elektronischen Ressource können nicht ausgeschlossen werden , Zusammenfassung in deutscher und englischer Sprache

Note: Intro -- Preface -- Contents -- 1: Introduction -- 2: The Cellular Structure of Actinobacteria -- 2.1 Diversity of Cell Morphology in Actinobacteria -- 2.1.1 Mycelium -- 2.1.2 Resistant Form of the Cells -- 2.2 Cell Envelope -- 2.2.1 Plasma Membrane -- 2.2.2 Cell Wall -- 2.2.3 Surface Layer and Capsule -- 2.3 Cytoplasm -- 2.3.1 Cytoskeleton -- 2.3.2 Inclusion Bodies -- 2.3.3 Bacterial Microcompartments (BMCs) -- 2.4 Other Cellular Structures -- 2.4.1 Vesicles -- 2.4.2 Flagella and Pili -- References -- 3: Growth and Life Cycle of Actinobacteria -- 3.1 Life Cycle of Actinobacteria -- 3.2 Differentiation in Actinobacteria -- 3.2.1 Aerial Growth -- 3.2.2 Developmental Regulators -- 3.2.3 Sporulation -- 3.2.3.1 Sporulation-Specific Cell Division -- 3.2.3.2 Chromosome Segregation -- 3.2.3.3 Spore Maturation -- 3.2.3.4 Control of Streptomyces Sporulation -- 3.2.3.5 Spore Germination -- 3.2.3.6 Streptomyces Programmed Cell Death -- 3.2.4 Cell Division -- 3.2.5 Vegetative Septation -- 3.2.5.1 Reproductive Septation -- 3.2.5.2 Cell Division in Nonfilamentous Actinobacteria -- 3.3 Factors Affecting Growth and Differentiation in Actinobacteria -- References -- 4: Classification and Taxonomy of Actinobacteria -- 4.1 Current Status in Actinobacterial Taxonomy -- 4.2 Classic and Recent Criteria in Taxonomical Classification of Actinobacteria -- 4.3 Phenetic Classification -- 4.3.1 Microscopic and Macroscopic Morphology -- 4.4 Physiological/Metabolic Characteristics -- 4.4.1 Nutritional Requirements -- 4.4.2 Growth Conditions -- 4.4.2.1 Temperature -- 4.4.2.2 pH -- 4.4.2.3 NaCl Tolerance -- 4.4.3 Antibiotic Sensitivity -- 4.4.4 Enzymatic Activity and Degradation Activity -- 4.5 Molecular Classification -- 4.5.1 16S rRNA Gene Sequence -- 4.5.2 Alternative Genes for Phylogenetic Analysis of Actinobacteria. , 4.5.3 DNA-DNA Hybridization and ANI Value -- 4.5.4 Whole Genome Sequencing -- 4.5.5 Phylogeny of Actinobacteria Based on Whole Genome Analysis -- 4.5.6 Molecular Typing -- 4.5.6.1 Pulsed-Field gel Electrophoresis (PFGE) -- 4.5.6.2 Multilocus Sequence Typing (MLST) -- 4.5.6.3 Random Amplified Polymorphism Deoxyribonucleic Acid (RAPD) -- 4.5.6.4 Ribotyping -- 4.5.6.5 MALDI-TOF Mass Spectrometry -- 4.6 Chemical Classification -- 4.6.1 Cell Wall Chemical Composition -- 4.6.2 Cell Membrane Isoprenoid Quinones -- 4.6.3 Cell Membrane Phospholipids -- 4.6.4 Cell Membrane Fatty Acid Pattern -- 4.6.5 Cell Membrane Mycolic Acid Type -- References -- 5: The Genetic System of Actinobacteria -- 5.1 Introduction -- 5.2 Sequencing Technologies to Determine the Genetics of Actinobacteria and the General Features of Their Genomes -- 5.3 Reporter Genes for Actinobacteria -- 5.4 Vectors for Mycelial Actinobacteria -- 5.5 Genetic Toolkit for the Manipulation of Mycelial Actinobacteria -- 5.5.1 Site-Specific Recombination Tools -- 5.5.2 Iterative Marker-Free Excision System -- 5.5.3 Transposon Mutagenesis in Mycelial Actinobacteria -- 5.5.4 Programmed Endonucleases, Cas9 -- 5.5.5 Controlling Elements for Transcription Regulation -- References -- 6: Ecology and Habitat Distribution of Actinobacteria -- 6.1 Introduction -- 6.2 Actinobacteria in Natural and Man-Made Environments -- 6.3 Actinobacteria in Terrestrial Habitats -- 6.4 Actinobacteria in Aquatic and Marine Habitats -- 6.5 Actinobacteria in Extreme Habitats -- 6.6 Phages of Actinobacteria -- 6.7 Conclusions: Impact of Molecular Advances on Actinobacterial Ecology and Future Directions -- References -- 7: Physiology of Actinobacteria -- 7.1 Introduction -- 7.2 Growth Requirements -- 7.2.1 Carbon Sources -- 7.2.1.1 Carbohydrate-Degrading Enzymes -- 7.2.1.2 Carbohydrate Uptake. , 7.2.2 Nitrogen Sources -- 7.2.2.1 Proteases and Peptidases and Amino Acid Transport -- 7.2.2.2 Sources of Ammonium and Ammonium Assimilation -- 7.2.3 Phosphorus Uptake and Regulation -- 7.3 Primary Metabolism -- 7.3.1 Carbohydrate Catabolism -- 7.3.2 Carbon Catabolite Repression and Stringent Response -- 7.3.3 Carbon Storage Compounds -- 7.3.4 Nitrogen Metabolism -- 7.3.4.1 Amino Acid Catabolism -- 7.3.4.2 Nucleotide Catabolism -- 7.3.4.3 Nitrogen Metabolite Biosynthesis -- 7.4 Secondary Metabolites -- References -- 8: Regulation of Secondary Metabolites of Actinobacteria -- 8.1 Introduction -- 8.2 Growth Rate and Nutritional Control During Secondary Metabolite Production -- 8.2.1 Influence of Phosphate on Antibiotic Production -- 8.2.2 Influence of Carbon on the Secondary Metabolite Production -- 8.2.2.1 Carbon Catabolic Repression by Glucose in Streptomycetes -- 8.2.2.2 Influence of Glucose on Secondary Metabolite Production -- 8.3 Regulatory Aspects of Nitrogen Metabolism -- 8.4 Influence of Nitrogen Sources on the Regulation of Secondary Metabolite Production -- 8.5 Signaling Molecules Governing Antibiotic Biosynthesis -- 8.5.1 γ-Butyrolactone Signaling -- 8.5.2 Antibiotics as Signaling Molecules -- 8.5.3 Interspecies Signaling in Streptomycetes -- 8.5.4 Positive Control Mechanisms -- 8.5.4.1 Two-Component Systems -- 8.5.4.2 One-Component Systems -- SARPs -- Interaction of Multiple Positive Regulators -- 8.5.5 Negative Control Mechanisms -- 8.5.6 Hierarchical Signaling Cascades -- 8.6 Induction of Silent Secondary Metabolite Clusters by Manipulating Gene Regulation -- 8.6.1 Induction of Silent Secondary Metabolite Clusters in the Native Host -- 8.6.1.1 Nontargeted Approaches to Induce Expression of Silent Clusters in the Native Producers. , 8.6.1.2 Targeted Approaches to Induce Expression of Silent Clusters in the Native Producers -- 8.6.2 Induction of Silent Secondary Metabolite Clusters by Heterologous Expression -- References -- 9: Symbiosis and Pathogenicity of Actinobacteria -- 9.1 Actinobacterial Symbiosis with Microorganisms and Insects -- 9.1.1 Actinobacterial Symbiosis with Microorganisms -- 9.1.2 Actinobacterial Symbiosis with Insects -- 9.1.2.1 Actinobacterial Nutritional Interaction with Insects -- 9.1.2.2 The Relationship Between Actinobacteria and Fungus-­Growing Insects -- 9.1.2.3 Symbiont Actinobacteria Protect the Insect Host Against Pathogens -- 9.2 Symbiosis and Pathogenicity in Human -- 9.2.1 Actinobacterial Symbiosis with Human -- 9.2.2 Actinobacterial Human Diseases -- 9.2.2.1 Actinomycetoma -- 9.2.2.2 Nocardiosis -- 9.2.2.3 Actinomycosis -- 9.2.2.4 Whipple Disease -- 9.2.2.5 Corynebacterium Infections -- 9.2.2.6 Mycobacterium tuberculosis -- 9.2.2.7 Nontuberculous Mycobacterial Infections -- 9.3 Actinobacterial Symbiosis and Pathogenicity in Animals -- 9.3.1 Actinobacterial Symbiosis with Animals -- 9.3.2 Actinobacterial Diseases in Animals -- 9.3.2.1 Animal Nocardiosis -- 9.3.2.2 Dermatophilosis -- 9.3.2.3 Caseous Lymphadenitis in Sheep and Goats -- 9.3.2.4 Nocardioform Placentitis in Horses -- 9.4 Actinobacterial Symbiosis and Pathogenicity with Plants -- 9.4.1 Actinobacterial Symbiosis with Plants -- 9.4.2 Actinobacterial Diseases in Plants -- References -- 10: The Role of Actinobacteria in Biotechnology -- 10.1 Color Codes of Biotechnology -- 10.2 Actinobacteria and Red Biotechnology -- 10.2.1 Antibacterial Agents -- 10.2.1.1 The "Golden Era" -- 10.2.1.2 The Next Generations -- 10.2.1.3 Oldie Approach -- 10.2.1.4 Siderophores -- 10.2.1.5 Conclusion and Outlook -- 10.2.2 Antifungal Agents. , 10.2.3 Antiviral Agents: The Labyrinthopeptin Story -- 10.2.4 Antitumor Agents -- 10.2.4.1 Cytostatics -- 10.2.4.2 Toxins for Immunoconjugates -- 10.2.5 Immunosuppressive Agents -- 10.2.6 Antiparasite Agents -- 10.2.7 Enzyme Inhibitors -- 10.2.7.1 Enzyme Inhibitors: Products from Satoshi Omura's and Hamano Umezawa's Groups -- 10.2.7.2 α-Glucosidase Inhibitor Acarbose -- 10.3 Actinobacteria and White Biotechnology -- 10.3.1 Enzymes -- 10.3.1.1 Proteases -- 10.3.1.2 Amylases -- 10.3.1.3 Xylanases -- 10.3.1.4 Cellulases -- 10.3.1.5 Other Enzymes -- 10.3.2 Organic Acids -- 10.3.3 Microbial Biotransformation -- 10.3.4 Biofuel -- 10.4 Actinobacteria and Green Biotechnology -- 10.4.1 Biocontrol -- 10.4.2 Herbicides and Insecticides -- 10.4.3 Animal Growth Promoters -- 10.5 Actinobacteria and Yellow Biotechnology -- 10.5.1 Vitamins -- 10.5.2 Amino Acids -- 10.6 Actinobacteria and Blue Biotechnology -- 10.6.1 Aquaculture -- 10.6.2 Antifouling Compounds -- 10.7 Actinobacteria and Gray Biotechnology -- 10.7.1 Recycling of Organic Compounds -- 10.7.2 Bioremediation of Toxic Agents -- 10.7.2.1 Bioremediation of Heavy Metals -- 10.7.2.2 Bioremediation of Pesticides -- 10.7.2.3 Bioremediation of Polycyclic Aromatic Hydrocarbons (PAHs) -- 10.7.3 Protection from Corrosion -- 10.8 Actinobacteria and Gold Biotechnology -- 10.8.1 Bioinformatics -- 10.8.2 Production of Nanoparticles (NPs) -- References -- 11: Practical Aspects of Working with Actinobacteria -- 11.1 Morphological Investigation -- 11.1.1 Macroscopic -- 11.1.1.1 The Aerial Mycelium and Its Color -- 11.1.1.2 Color of the Substrate Mycelium and the Soluble Pigments -- 11.1.2 Microscopic Analyses -- 11.1.2.1 Formation of Sporangia -- 11.1.2.2 Formation of Spore Chains and the Spore Surface Ornamentation -- 11.1.2.3 Light Microscopic Characterization. , 11.1.2.4 Scanning Electron Microscopy.