Ribonucleases : structures and functions / edited by Giuseppe D'Alessio, James F. Riordan.

Format:

Book

Contributor:

D'Alessio, Giuseppe.

Riordan, James F., 1934-

Language:

English

Subjects (All):

Ribonucleases--Structure-activity relationships.

Ribonucleases.

Nucleases.

Physical Description:

1 online resource (699 p.)

Place of Publication:

San Diego : Academic Press, c1997.

Language Note:

English

Summary:

Pancreatic ribonuclease, the focus of highly productive scientific research for more than half a century and the only enzyme to be the basis of four Nobel prizes, has recently undergone a resurgence in popularity for the recognition of an extended ribonuclease superfamily with functions ranging from tumour growth and inhibition to self-recognition and neurotoxicity. This volume highlights the functional diversity of ribonucleases and reveals the emerging research opportunities provided by these enzymes.* Never before has discussion of the entire family of ribonucleases and related

Contents:

Front Cover; Ribonucleases Structures and Functions; Copyright Page; Contents; Contributors; Preface; Chapter 1. Escherichia coli Ribonucleases: Paradigms for Understanding Cellular RNA Metabolism and Regulation; I. Introduction; II. Gallery of Escherichia Coli Ribonucleases; III. Endoribonucleases; IV. Exoribonucleases; V. Ribonuclease Functional Roles; VI. Other Ribonucleases; VII. Ribonuclease Regulation an RNA Metabolic Control; VIII. Conclusions and Prospects; References; Chapter 2. Barnase and Barstar; I. Introduction; II. Gene Structure; III. Activity and Structure

IV. Barnase, Barstar, and the Folding ProblemV. Barnase and Barstar Homologs; VI. Other Practical Applications of Barnase; VII. Concluding Remarks; References; Chapter 3. RNase T1/RNase T2 Family RNases; I. RNase T1 Family RNases; II. RNase T2 Family RNases; References; Chapter 4. Structure and Mechanism of Action of Cytotoxic Ribonuclease a-Sarcin; I. Discovery of a-Sarcin and Determination of Basis of Its Cytotoxicity; II. Substrate Specificity of a-Sarcin; III. a-Sarcin Cleavage Site Sequence; IV. Structure of a-Sarcin and of Related Aspergillus Toxins

V. Mechanism by Which a-Sarcin Enters CellsVI. a-Sarcin Recognition Elements in 28S rRNA; VII. Conformation of Sarcin Domain in 28S rRNA; VIII. Effect of Mutations of Analog of G4319 in 28S rRNA on Recognition Oligoribonucleotides by a-Sarcin; IX. Phenotype of Mutations in G2655 in Escherichia coli 23S rRNA; X. Relationship of a-Sarcin RNA Identity Element to Selection by Toxin of Unique Site of Phosphodiester Bond Hydrolysis; XI. Three-Dimensional Structure of Restrictocin, a Homolog of a-Sarcin. Binding to a-Sarcin Domain RNA and Catalytic Mechanism; XII. Coda; References

Chapter 5. Plant RibonucleasesI. Introduction; II. Classes of Plant RNases; III. Regulation and Functions of Plant RNases; IV.Conclusions and Future Prospects; References; Chapter 6. S-RNases and Other Plant Extracellular Ribonucleases; I. Introduction; II. Self-Incompatibility in the Solanaceae; III. S-RNases from the Rosaceae; IV. Extracellular Ribonucleases Associated with Stress; V. Seed RNases and Other RNases of Unknown Function and Location; VI. Plant Extracellular RNases: Enzymes in Search of a Substrate; References; Chapter 7. Evolutionary Reconstructions in the Ribonuclease Family

I. IntroductionII. Protein Engineering to Understand Evolution; III. Reconstructing Evolution of Biomolecular Behavior in RNase Superfamily; IV. Repair of Damaged Pseudogenes by Gene Conversion: A Mechanism for Obtaining Biomolecular Function in Proteins; V. Physiological Function of Seminal RNase; VI. Conclusions; References; Chapter 8. Evolution of Vertebrate Ribonucleases: Ribonuclease A Superfamily; I. The Ribonuclease Superfamily; II. Mammalian Ribonucleases 1: Pancreatic Type; References; Chapter 9. Pancreatic Ribonucleases; I. Introduction

II. Reaction Catalyzed by Pancreatic Ribonucleases

Notes:

Description based upon print version of record.

Includes bibliographical references and index.

ISBN:

1-281-03353-7

9786611033538

0-08-054059-7

OCLC:

476109716