| Literature DB >> 27464500 |
Hans A V Kistemaker1, Aurelio Pio Nardozza2, Herman S Overkleeft1, Gijs A van der Marel1, Andreas G Ladurner3,4,5, Dmitri V Filippov6.
Abstract
Mono-ADP-ribosylation is a dynamic posttranslational modification (PTM) with important roles in signaling. Mammalian proteins that recognize or hydrolyze mono-ADP-ribosylated proteins have been described. We report the synthesis of ADP-ribosylated peptides from the proteins histone H2B, RhoA and, HNP-1. An innovative procedure was applied that makes use of pre-phosphorylated amino acid building blocks. Binding assays revealed that the macrodomains of human MacroD2 and TARG1 exhibit distinct specificities for the different ADP-ribosylated peptides, thus showing that the sequence surrounding ADP-ribosylated residues affects the substrate selectivity of macrodomains.Entities:
Keywords: ADP-ribosylation; peptides; posttranslational modifications; proteins; solid-phase synthesis
Mesh:
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Year: 2016 PMID: 27464500 DOI: 10.1002/anie.201604058
Source DB: PubMed Journal: Angew Chem Int Ed Engl ISSN: 1433-7851 Impact factor: 15.336