The language of covalent histone modifications

Author: Strahl, B.D.; Allis, C.D.

Description: Histone proteins and the nucleosomes they form with DNA are the fundamental building blocks of eukaryotic chromatin. A diverse array of post-translational modifications that often occur on tail domains of these proteins has been well documented. Although the function of these highly conserved modifications has remained elusive, converging biochemical and genetic evidence suggests functions in several chromatin-based processes. We propose that distinct histone modifications, on one or more tails, act sequentially or in combination to form a ‘histone code’ that is, read by other proteins to bring about distinct downstream events.

Subject headings: Acetylation; Amino Acid Sequence; Animals; Chromatin/physiology; Histones/chemistry/metabolism/physiology; Humans; Lysine/physiology; Microtubules/physiology; Models, Biological; Molecular Sequence Data; Phosphorylation; Protein Processing, Post-Translational; Serine/metabolism

Publication year: 2000

Journal or book title: Nature

Volume: 403

Issue: 6765

Pages: 41-45

Find the full text : http://www.gs.washington.edu/academics/courses/braun/55104/readings/strahl.pdf

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Type: Journal Article

Serial number: 1988