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Protein methyltransferases / edited by Steven G. Clarke, Fuyuhiko Tamanoi.
- Format:
- Book
- Series:
- Enzymes ; v. 24.
- The enzymes ; v. 24
- Language:
- English
- Subjects (All):
- Methyltransferases.
- Proteins--Methylation.
- Proteins.
- Physical Description:
- 1 online resource (599 p.)
- Place of Publication:
- Amsterdam ; London : Academic Press, c2006.
- Language Note:
- English
- Summary:
- Protein methylation has recently emerged as one of the most exciting areas of study on posttranslational modification. A large family of protein methyltransferases has been identified and their structural properties have been characterized. These studies have provided novel insights into how methylation regulates a variety of biological functions including DNA and RNA metabolism, protein synthesis and signal transduction. Methylation also plays important roles in aging. This volume is intended to capture these recent developments concerning protein methyltransferases.
- Contents:
- Front cover; Title page; Copyright; Table of contents; Front matter; Preface; Body; Part I Overview of Protein Methyltransferases; 1 Protein Methyltransferases:Their Distribution Among the Five Structural Classes of AdoMet-Dependent Methyltransferases; I. Abstract; II. Introduction; III. Class I MTases: In the Beginning, an MTase Was an MTase Was an MTase; IV. Class II MTases: A Lesson in Cobalamin; V. Class III MTases: Another Lesson in Cobalamin; VI. Class IV MTases: Knotty New Structure SPOUTs; VII. Class V MTases: Pseudo Knotty Structures Come in SETs
- VIII. Conformations of AdoMet and AdoHcyIX. Diverse Set of Mechanisms for a Conserved Class of MTase; X. Conclusions; Part II Modification of Lysine and Arginine Residues in Signal Transduction, Transcription, Translation, and Other Functions; 2 The Family of Protein Arginine Methyltransferases; I. Abstract; II. Introduction; III. The Protein Arginine Methyltransferases Family of Enzymes; IV. Mammalian Protein Arginine Methyltransferases; V. Yeast Protein Arginine Methyltransferases; VI. PRMT Substrate Specificity; VII. Small-Molecule Inhibitors of Protein Arginine Methyltransferases
- 3 Diverse Roles of Protein Arginine MethyltransferasesI. Abstract; II. Introduction; III. Arginine Methylation and Intermolecular Interactions; IV. Roles of PRMTs in Cellular Processes; V. Roles of Protein Arginine Methyltransferases in Development and Differentiation; VI. Roles of Protein Arginine Methyltransferases in Disease; VII. Conclusions and Future Directions; 4 Structure of Protein Arginine Methyltransferases; I. Abstract; II. Protein Arginine Methylation; III. PRMT1; IV. CARM1/PRMT4; V. A Conserved PRMT Core; VI. Structure of the Conserved PRMT Core
- VII. PRMT Dimerization is Essential for AdoMet Binding and Enzymatic ActivityVIII. Multiple Substrate Binding Grooves; IX. Asymmetric and Symmetric Dimethylarginines; X. Antagonize Arginine Methylation; 5 Methylation and Demethylation of Histone Arg and Lys Residues in Chromatin Structure and Function; I. Abstract; II. Introduction; III. Chromatin Structure and Function; IV. Histone Lys Methylation; V. Histone Lys Demethylase; VI. Histone Arg Methylation and Transcription; VII. Histone Arg Demethylating Enzymes; VIII. Conclusions; 6 Structure of SET Domain Protein Lysine Methyltransferases
- I. AbstractII. Introduction; III. SET Domains in Context; IV. Overall Structure; V. Structure of the N- and C-Flanking Domains; VI. The Cofactor Binding Site; VII. Substrate Binding; VIII. Active Site and Methylation; IX. Flexibility of the C-Flanking Domain; 7 Non-Histone Protein Lysine Methyltransferases: Structure and Catalytic Roles; I. Abstract; II. Introduction; III. Diversity of Polypeptide Substrates; IV. Non-Histone Protein Methyltransferases; V. Conclusions and Future Prospects; 8 Demethylation Pathways for Histone Methyllysine Residues; I. Abstract; II. Introduction
- III. Histone Demethylation by LSD1 Is a Flavin-Dependent Oxidative Process
- Notes:
- Description based upon print version of record.
- Includes bibliographical references and indexes.
- ISBN:
- 1-280-64133-9
- 9786610641338
- 0-08-046042-9
- OCLC:
- 476002711
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