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Microorganisms as Model Systems for Studying Evolution

The microorganisms present on the earth today possess a vast range of metabolic activities and are often able to demonstrate their surprising versatility by gaining both new enzyme activities and new metabolic path­ ways through mutations. It is generally assumed that the earliest micro­ organisms w...

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Bibliographic Details
Other Authors: Mortlock, Robert (Editor)
Format: eBook
Language:English
Published: New York, NY Springer US 1984, 1984
Edition:1st ed. 1984
Series:Monographs in Evolutionary Biology
Subjects:
Evolutionary Biology
Evolution (biology)
Online Access:
Collection: Springer Book Archives -2004 - Collection details see MPG.ReNa
Table of Contents:
  • 3. Bipolar Transcription of the Pentitol Operons
  • 4. The Pentitol Operon Enzymes
  • 5. Substrate Specificity of the Pentitol Operon Enzymes
  • 6. rbt Messenger RNA
  • 7. DNA Sequencing of the Pentitol Operons
  • 8. Translation of the Two Kinases
  • 9. Invert Repeat Sequences Enclose the Two Operons
  • 10. Structure of an Experimentally Evolved Gene Duplication
  • 11. Evolutionary Lessons from the Pentitol Operons
  • References
  • 4 The Development of Catabolic Pathways for the Uncommon Aldopentoses
  • 1. The Structure of the Aldopentoses and Their Occurrence in Nature
  • 2. The Pathways of Degradation of Aldopentoses by Coliform Bacteria
  • 3. The Biochemical and Genetic Bases for the Establishment of New Enzymatic Pathways for the Degradation of Aldopentoses
  • 4. Summary
  • References
  • 5 Functional Divergence of theL-Fucose System in Mutants of Escherichia coli
  • 1. Introduction
  • 2. Reversibility of NAD-Linked Reactions
  • 1 The Utilization of Pentitols in Studies of the Evolution of Enzyme Pathways
  • 1. Introduction
  • 2. The Pentitols
  • 3. The Utilization of Pentitols by Klebsiella Species
  • 4. The Origin of the l-Arabitol Dehydrogenase Activity
  • 5. Mutations Improving the Growth Rate on Xylitol
  • 6. The Growth of Escherichia Coli Strains on Xylitol
  • 7. The Utilization of Xylitol by a Mutant in the Genus Erwinia
  • 8. Summary
  • References
  • 2 Experimental Evolution of Ribitol Dehydrogenase
  • 1. Introduction
  • 2. Pentitol Metabolism in Klebsiella aerogenes
  • 3. Chemostat Culture of Klebsiella aerogenes on Xylitol
  • 4. Evolution of Ribitol Dehydrogenase in the Chemostat
  • 5. Fluctuating Selective Pressure
  • 6. Transfer of the Klebsiella aerogenes Ribitol Dehydrogenase Gene into Escherichia coli K12
  • 7. Evolutionary Lessons from the Chemostat Studies
  • References
  • 3 The Structure and Control of the Pentitol Operons
  • 1. Introduction
  • 2. The Structure of ?p rbt and ?p rbt dal
  • 1. The Leucine Operon in Salmonella typhimurium Wild-Type Strains
  • 2. The Wild-Type Isopropylmalate Isomerase
  • 3. Strains Carrying leuD Mutations Revert to Leucine Prototrophy
  • 4. Model for Leucine Biosynthesis in leuD—supQ Mutant Strains
  • 5. Leucine Biosynthesis in leuD—supQ Mutant Strains
  • 6. Genetic Characterization of the leuD—newD Isopropylmalate Isomerase
  • 7. Biochemical Characterization of the leuC—newD Isopropylmalate Isomerase
  • 8. Theoretical Steps in the Evolution of a Complex Enzyme
  • 9. Characterization of the newD (and supQ) Gene(s)
  • References
  • 10 Arrangement and Rearrangement of Bacterial Genomes
  • 1. Introduction
  • 2. Chromosomal Rearrangements: Mechanisms of Change
  • 3. Conservation of Global Gene Order: Mechanisms of Stability
  • 4. Conclusion
  • References
  • 3. A Mutant That Uses an NAD-Linked Dehydrogenase to Grow on l-1,2-Propanediol
  • 4. Biochemistry of the Fucose System
  • 5. Enzymic Changes in the Fucose System in Mutants and Revertants
  • 6. Genetic Organization and Regulation of the Fucose System
  • 7. Sequential Mutations Changing Propanediol and Fucose Utilization
  • 8. Relationship of the Fucose and the Rhamnose Systems
  • 9. Conversion of the Fucose System for d-Arabinose Utilization
  • 10. Propanediol-Positive Mutants as Evolutionary Vanguards
  • 11. Retrospective and Prospective Views
  • References
  • 6 The Evolved ?-Galactosidase System of Escherichia coli
  • 1. Introduction
  • 2. Development of the Evolved ?-Galactosidase System as a Tool for Studying Evolution
  • 3. Evolution of Multiple Functions for Evolved ?-Galactosidase Enzyme: An Evolutionary Pathway
  • 4. Kinetic Analysis of Evolved ?-Galactosidase Enzymes
  • 5. Evolution by Intragenic Recombination
  • 6. Allolactose Synthesis: Another New Function for Class IV Enzyme
  • 7. The Role of Regulatory Mutations in the Evolution of Lactose Utilization
  • 8. Directed Evolution of a Repressor
  • 9. The Fully Evolved EBG Operon
  • 10. A Model for Evolution in Diploid Organisms
  • 11. Future Perspectives
  • References
  • 7 Amidases of Pseudomonas aeruginosa
  • 1. Introduction
  • 2. Amidase Regulatory Mutants
  • 3. Amidase-Negative Mutants
  • 4. Mutants with Altered Enzymes
  • 5. Properties of Wild-Type and Mutant Amidases
  • 6. Amidase Genes and Enzymes
  • References
  • 8 Structural Evolution of Yeast Alcohol Dehydrogenase in the Laboratory
  • 1. Introduction
  • 2. The Biochemistry and Regulation of Yeast Alcohol Dehydrogenase
  • 3. The Mechanism of Allyl Alcohol Resistance
  • 4.Amino Acid Substitutions in the Mutant ADHs
  • 5. Altered Kinetics of the Mutants
  • 6. Evolutionary Implications
  • References
  • 9 Gene Recruitment for a Subunit of Isopropylmalate Isomerase

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