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New functions for an ancient domain

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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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Figure 1: Macrodomains bind metabolites of NAD+.
Figure 2: Macrodomain-containing proteins in humans.
Figure 3: Macrodomains are ancient and highly conserved structural domains that bind metabolites of NAD+.

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Acknowledgements

The author would like to thank C. Danko for assistance with the bioinformatics analysis of the macrodomain-containing proteins (Fig. 2), and N. Hah and J. Seckute for assistance with rendering the X-ray crystal structures (Fig. 3).

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Authors and Affiliations

  1. W. Lee Kraus is in the Department of Molecular Biology and Genetics, and the Department of Pharmacology, Cornell University, Ithaca, New York, USA, Weill Medical College of Cornell University, New York, New York, USA.,

    W Lee Kraus

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Kraus, W. New functions for an ancient domain. Nat Struct Mol Biol 16, 904–907 (2009). https://doi.org/10.1038/nsmb0909-904

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