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Synthesis and Macrodomain Binding of Mono-ADP-Ribosylated Peptides.
- Source :
-
Angewandte Chemie (International ed. in English) [Angew Chem Int Ed Engl] 2016 Aug 26; Vol. 55 (36), pp. 10634-8. Date of Electronic Publication: 2016 Jul 28. - Publication Year :
- 2016
-
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.<br /> (© 2016 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.)
- Subjects :
- DNA Repair Enzymes chemistry
DNA Repair Enzymes metabolism
Histones chemistry
Histones metabolism
Humans
Hydrolases chemistry
Hydrolases metabolism
Peptides chemistry
Peptides metabolism
Protein Binding
Protein Domains
Thiolester Hydrolases chemistry
Thiolester Hydrolases metabolism
alpha-Defensins chemistry
alpha-Defensins metabolism
rhoA GTP-Binding Protein chemistry
rhoA GTP-Binding Protein metabolism
ADP-Ribosylation
Histones chemical synthesis
Peptides chemical synthesis
Solid-Phase Synthesis Techniques methods
alpha-Defensins chemical synthesis
rhoA GTP-Binding Protein chemical synthesis
Subjects
Details
- Language :
- English
- ISSN :
- 1521-3773
- Volume :
- 55
- Issue :
- 36
- Database :
- MEDLINE
- Journal :
- Angewandte Chemie (International ed. in English)
- Publication Type :
- Academic Journal
- Accession number :
- 27464500
- Full Text :
- https://doi.org/10.1002/anie.201604058