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The macro domain is an ADP-ribose binding module

2005; Springer Nature; Volume: 24; Issue: 11 Linguagem: Inglês

10.1038/sj.emboj.7600664

1460-2075

Georgios I. Karras, Georg Kustatscher, Heeran R Buhecha, Mark D. Allen, Céline Pugieux, Fiona Sait, Mark Bycroft, Andreas G. Ladurner,

Toxin Mechanisms and Immunotoxins

The ADP-ribosylation of proteins is an important post-translational modification that occurs in a variety of biological processes, including DNA repair, transcription, chromatin biology and long-term memory formation. Yet no protein modules are known that specifically recognize the ADP-ribose nucleotide. We provide biochemical and structural evidence that macro domains are high-affinity ADP-ribose binding modules. Our structural analysis reveals a conserved ligand binding pocket among the macro domain fold. Consistently, distinct human macro domains retain their ability to bind ADP-ribose. In addition, some macro domain proteins also recognize poly-ADP-ribose as a ligand. Our data suggest an important role for proteins containing macro domains in the biology of ADP-ribose.