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.

Author affiliations

1. Robert J. Sims 3rd is at Constellation Pharmaceuticals, 148 Sidney Street, Cambridge, Massachusetts 02139, USA.
   Email: roberts@constellationpharma.com
2. Danny Reinberg is at the Howard Hughes Medical Institute, New York University School of Medicine-Smilow Research Center, Biochemistry Department, 522 First Avenue, 2nd Floor, Room 211, New York, New York 10016, USA.
   Email: reinbd01@nyumc.org

Published online 11 September 2008

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