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

Nature Reviews Molecular Cell BiologyPublished 11 September 2008
Robert J. Sims, Danny Reinberg
Citations287
SJR quartileQ1
SJR score37.35
SNIP20.23

TL;DR

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, reminiscent of other regulatory cascades in transcription and cell signalling.

Abstract

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.

Keywords

Biochemistry, Genetics and Molecular Biology