Description
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.
Readership
Biochemists, cell biologists, molecular biologists, biophysicists, and microbiologists
The Enzymes, 1st Edition
The Enzymes, Volume 24 Table of Contents
Protein methyltransferases
Part I: Overview of Protein Methyltransferases
1. Protein methyltransferases: Their distribution among the five structural classes of AdoMet-dependent methyltransferases
Part II: Modification of Lysine and Arginine Residues in Signal Transduction, Transcription Translation, and Other Functions
2. The family of protein arginine methyltransferases
3. Diverse roles of protein arginine methyltransferases
4. Structure of protein arginine methyltransferases
5. Methylation and demethylation of histone Arg and Lys residues in chromatin structure and function
6. Structure of SET domain protein lysine methyltransferases
7. Non-histone protein lysine methyltransferases - structure and catalytic roles
8. Demethylation pathways for histone methyllysine residues
Part III: Biological Regulation by Protein Methyl Ester Formation
9. Structure and function of isoprenylcysteine carboxylmethyltransferase (Icmt), a key enzyme in CaaX processing
10. Genetic approaches for understanding the physiologic importance of the carboxyl methylation of isoprenylated proteins
11. Reversible methylation of protein phosphatase 2A
12. Reversible methylation of glutamate residues in the receptor proteins of bacterial sensory systems
Part IV: Recognition of Damaged Proteins in Aging by Protein Methyltransferases
13. Protein L-isoaspartyl, D-aspartyl O-methyltransferases:
catalysts for protein repair
Part V: Modification of Proteins by Methylation of Glutamine and Asparagine Residues
14. Modification of glutamine residues in proteins involved in translation
15. Modification of phycobiliproteins at asparagine residues
Part VI: Inhibition of Metyltransferases by Metabolites
16. Inhibition of mammalian protein methyltransferases by 5'-methylthioadenosine (MTA): A mechanism of action of dietary SAMe?
