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Nature Structural & Molecular Biology 16, 904 - 907 (2009)
doi:10.1038/nsmb0909-904
New functions for an ancient domain
W Lee Kraus1
- W. Lee Kraus is in the Department of Molecular Biology and Genetics, Cornell University, Ithaca, New York, USA, and the Department of Pharmacology, Weill Medical College of Cornell University, New York, New York, USA.
Correspondence to: W Lee Kraus1 e-mail: wlk5@cornell.edu
Abstract
Macrodomains function as binding modules for metabolites of NAD+, including poly(ADP-ribose). Three new studies explore how binding of poly(ADP-ribose) by the macrodomains of histone variant macroH2A1.1 and the ATP-dependent chromatin-remodeling protein ALC1 (also called CHD1L) leads to the modulation of chromatin structure, regulating nuclear functions such as DNA-damage detection and repair.
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