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Progress
Nature 403, 41-45 (6 January 2000) | doi:10.1038/47412
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Physician / Senior Physician - Clinical Unit, Drug Discovery, R&D
- GlaxoSmithKline
- Cambridge, United Kingdom
Laboratory Technician (Pharmaceutical Analysis & Quality Control)
- Alliance Institute of Advanced Pharmacy and Health Sciences
- Hyderabad 500038 India
The language of covalent histone modifications
Brian D. Strahl & C. David Allis
Abstract
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.
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