Is there a code embedded in proteins that is based on post-translational modifications?

被引：236

作者：

Sims, Robert J., III ^{[1
]}

Reinberg, Danny ^{[2
]}

机构：

[1] Constellat Pharmaceut, Cambridge, MA 02139 USA

[2] NYU, Sch Med, Howard Hughes Med Inst, Smilow Res Ctr,Biochem Dept, New York, NY 10016 USA

来源：

NATURE REVIEWS MOLECULAR CELL BIOLOGY | 2008年 / 9卷 / 10期

关键词：

D O I：

10.1038/nrm2502

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

Covalent post-translational modifications (PTMs) provide vast indexing potential and expanded protein use. The 'histone code' hypothesis has inspired rapid advances throughout chromatin biology, and has recently been tapped for its relevance to non- histone proteins. Comprehensive analyses suggest that rather than constituting a general code, the covalent modifications of proteins (including histones) provide surfaces that are recognized by effectors that can give rise to intricate interactions and downstream events. These are reminiscent of other regulatory cascades in transcription and cell signalling.

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页码：815 / 820

页数：7

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