Structural dynamics of protein lysine methylation and demethylation

Xiaodong Cheng; Xing Zhang

doi:10.1016/j.mrfmmm.2006.05.041

Structural dynamics of protein lysine methylation and demethylation

Xiaodong Cheng, Xing Zhang

Research output: Contribution to journal › Article › peer-review

61 Scopus citations

Abstract

Lysine methylation plays a central role in the "histone code" that regulates chromatin structure, impacts transcription, and responds to DNA damage. A single lysine can be mono-, di-, tri-methylated, or unmethylated, with different functional consequences for each of the four forms. This review (written in the early 2006) described structural aspects of methylation of histone lysine residues by two enzyme families with entirely different structural scaffolding (the SET proteins and Dot1p), and the protein motifs that recognize (decode) these methyl-lysine signals. We also discuss the recently discovered protein lysine demethylating enzymes (LSD1 and JmjC domains).

Original language	English (US)
Pages (from-to)	102-115
Number of pages	14
Journal	Mutation Research - Fundamental and Molecular Mechanisms of Mutagenesis
Volume	618
Issue number	1-2
DOIs	https://doi.org/10.1016/j.mrfmmm.2006.05.041
State	Published - May 1 2007
Externally published	Yes

Keywords

Protein lysine methylation and demethylation
S-Adenosyl-l-methionine (AdoMet)
SET domain proteins

ASJC Scopus subject areas

Molecular Biology
Genetics
Health, Toxicology and Mutagenesis

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10.1016/j.mrfmmm.2006.05.041

Cite this

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title = "Structural dynamics of protein lysine methylation and demethylation",

abstract = "Lysine methylation plays a central role in the {"}histone code{"} that regulates chromatin structure, impacts transcription, and responds to DNA damage. A single lysine can be mono-, di-, tri-methylated, or unmethylated, with different functional consequences for each of the four forms. This review (written in the early 2006) described structural aspects of methylation of histone lysine residues by two enzyme families with entirely different structural scaffolding (the SET proteins and Dot1p), and the protein motifs that recognize (decode) these methyl-lysine signals. We also discuss the recently discovered protein lysine demethylating enzymes (LSD1 and JmjC domains).",

keywords = "Protein lysine methylation and demethylation, S-Adenosyl-l-methionine (AdoMet), SET domain proteins",

author = "Xiaodong Cheng and Xing Zhang",

note = "Funding Information: Work in our laboratory is supported in part by grants from the National Institute of Health (GM49245 and GM68680). X.C. is a Georgia Research Alliance Eminent Scholar.",

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AU - Cheng, Xiaodong

AU - Zhang, Xing

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AB - Lysine methylation plays a central role in the "histone code" that regulates chromatin structure, impacts transcription, and responds to DNA damage. A single lysine can be mono-, di-, tri-methylated, or unmethylated, with different functional consequences for each of the four forms. This review (written in the early 2006) described structural aspects of methylation of histone lysine residues by two enzyme families with entirely different structural scaffolding (the SET proteins and Dot1p), and the protein motifs that recognize (decode) these methyl-lysine signals. We also discuss the recently discovered protein lysine demethylating enzymes (LSD1 and JmjC domains).

KW - Protein lysine methylation and demethylation

KW - S-Adenosyl-l-methionine (AdoMet)

KW - SET domain proteins

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Structural dynamics of protein lysine methylation and demethylation

Abstract

Keywords

ASJC Scopus subject areas

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