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PubMed · 15902274

The macro domain is an ADP-ribose binding module.

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

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.

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Adenosine DiphosphateAdenosine Diphosphate RiboseAmino Acid SequenceArchaeal ProteinsArchaeoglobus fulgidusBinding SitesCalorimetry, Differential ScanningCarrier ProteinsCatalysisCrystallography, X-RayHistonesHumansHydrolysisLigandsModels, MolecularMolecular Sequence DataNeoplasm ProteinsPhosphoric Monoester HydrolasesPoly Adenosine Diphosphate RibosePoly(ADP-ribose) PolymerasesProtein BindingProtein ConformationProtein Structure, SecondaryProtein Structure, TertiaryRecombinant Fusion ProteinsSaccharomyces cerevisiae ProteinsSequence AlignmentSequence Homology, Amino AcidSpecies SpecificityStructure-Activity RelationshipComparative StudyJournal ArticleResearch Support, Non-U.S. Gov't

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Georgios I Karras, Georg Kustatscher, Heeran R Buhecha, Mark D Allen, Céline Pugieux, Fiona Sait, Mark Bycroft, Andreas G Ladurner. 2005-05-19. The macro domain is an ADP-ribose binding module.. https://doi.org/10.1038/sj.emboj.7600664

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