期刊
TRENDS IN BIOCHEMICAL SCIENCES
卷 38, 期 5, 页码 243-252出版社
ELSEVIER SCIENCE LONDON
DOI: 10.1016/j.tibs.2013.02.004
关键词
histone methylation; ribosomal protein methylation; PRMTs; SET-domain methyltransferases
资金
- US Public Health Service [GM026020]
Methylated lysine and arginine residues in histones represent a crucial part of the histone code, and recognition of these methylated residues by protein interaction domains modulates transcription. Although some methylating enzymes appear to be histone specific, many can modify histone and non-histone substrates and an increasing number are specific for non-histone substrates. Some of the non-histone substrates can also be involved in transcription, but a distinct subset of protein methylation reactions occurs at residues buried deeply in ribosomal proteins that may function in protein-RNA interactions rather than protein-protein interactions. Additionally, recent work has identified enzymes that catalyze protein methylation reactions at new sites in ribosomal and other proteins. These reactions include modifications of histidine and cysteine residues as well as the N terminus.
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