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PMID: 15869391 Published · ppublish English Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Review

Structural and sequence motifs of protein (histone) methylation enzymes.

Annual review of biophysics and biomolecular structure ·Vol. 34 ·2005-00-00 ·Pages 267-94

Cheng X, Collins RE, Zhang X

Abstract

With genome sequencing nearing completion for the model organisms used in biomedical research, there is a rapidly growing appreciation that proteomics, the study of covalent modification to proteins, and transcriptional regulation will likely dominate the research headlines in the next decade. Protein methylation plays a central role in both of these fields, as several different residues (Arg, Lys, Gln) are methylated in cells and methylation plays a central role in the "histone code" that regulates chromatin structure and impacts transcription. In some cases, a single lysine can be mono-, di-, or trimethylated, with different functional consequences for each of the three forms. This review describes structural aspects of methylation of histone lysine residues by two enzyme families with entirely different structural scaffolding (the SET proteins and Dot1p) and methylation of protein arginine residues by PRMTs.

MeSH Terms
Amino Acid Motifs Amino Acid Sequence Animals Arginine/chemistry Binding Sites Chromatin/chemistry Crystallography, X-Ray Histone-Lysine N-Methyltransferase/chemistry,metabolism Histones/chemistry Humans Lysine/chemistry Mass Spectrometry Methylation Models, Molecular Molecular Sequence Data Peptides/chemistry Phenylalanine/chemistry Protein Binding Protein Structure, Tertiary Proteins/chemistry Protons Sequence Homology, Amino Acid Tyrosine/chemistry Zinc/chemistry
Chemicals
Chromatin Histones Peptides Proteins Protons Tyrosine Phenylalanine Arginine Histone-Lysine N-Methyltransferase Zinc Lysine
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Cheng Xiaodong
Department of Biochemistry, Emory University School of Medicine, Atlanta, Georgia 30322, USA. xcheng@emory.edu
Collins Robert E
Zhang Xing
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Article Info
Journal
Annual review of biophysics and biomolecular structure
Abbr.
Annu Rev Biophys Biomol Struct
ISSN
1056-8700
DOI
10.1146/annurev.biophys.34.040204.144452
Email
xcheng@emory.edu
Published
2005-00-00
Pages
267-94
Language
English
Region
United States
NLM ID
9211097
PMCID
PMC2733851
Subset
IM
Grants
NIGMS NIH HHS · T32 GM08367 · United States
NIGMS NIH HHS · GM61355 · United States
NIGMS NIH HHS · T32 GM008367 · United States
NIGMS NIH HHS · R01 GM068680-01A2 · United States
NIGMS NIH HHS · R01 GM068680 · United States
NIGMS NIH HHS · GM49245 · United States
NIGMS NIH HHS · R01 GM049245 · United States
NIGMS NIH HHS · R01 GM061355 · United States
External Links
PubMed source DOI: 10.1146/annurev.biophys.34.040204.144452 PMC Full Text
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