Processing of protein ADP-ribosylation by Nudix hydrolases.

Autor: Palazzo L; Sir William Dunn School of Pathology, University of Oxford, Oxford, OX1 3RE, U.K., Thomas B; Sir William Dunn School of Pathology, University of Oxford, Oxford, OX1 3RE, U.K., Jemth AS; †Science for Life Laboratory, Division of Translational Medicine and Chemical Biology, Department of Medical Biochemistry and Biophysics, Karolinska Institutet, S-171 21 Stockholm, Sweden., Colby T; ‡Max Planck Institute for Biology of Ageing, Joseph-Stelzmann-Street 9b, D-50931 Köln/Cologne, Germany., Leidecker O; ‡Max Planck Institute for Biology of Ageing, Joseph-Stelzmann-Street 9b, D-50931 Köln/Cologne, Germany., Feijs KL; Sir William Dunn School of Pathology, University of Oxford, Oxford, OX1 3RE, U.K., Zaja R; Sir William Dunn School of Pathology, University of Oxford, Oxford, OX1 3RE, U.K., Loseva O; †Science for Life Laboratory, Division of Translational Medicine and Chemical Biology, Department of Medical Biochemistry and Biophysics, Karolinska Institutet, S-171 21 Stockholm, Sweden., Puigvert JC; †Science for Life Laboratory, Division of Translational Medicine and Chemical Biology, Department of Medical Biochemistry and Biophysics, Karolinska Institutet, S-171 21 Stockholm, Sweden., Matic I; ‡Max Planck Institute for Biology of Ageing, Joseph-Stelzmann-Street 9b, D-50931 Köln/Cologne, Germany., Helleday T; †Science for Life Laboratory, Division of Translational Medicine and Chemical Biology, Department of Medical Biochemistry and Biophysics, Karolinska Institutet, S-171 21 Stockholm, Sweden., Ahel I; Sir William Dunn School of Pathology, University of Oxford, Oxford, OX1 3RE, U.K.
Jazyk: angličtina
Zdroj: The Biochemical journal [Biochem J] 2015 Jun 01; Vol. 468 (2), pp. 293-301.
DOI: 10.1042/BJ20141554
Abstrakt: ADP-ribosylation is a post-translational modification (PTM) of proteins found in organisms from all kingdoms of life which regulates many important biological functions including DNA repair, chromatin structure, unfolded protein response and apoptosis. Several cellular enzymes, such as macrodomain containing proteins PARG [poly(ADP-ribose) glycohydrolase] and TARG1 [terminal ADP-ribose (ADPr) protein glycohydrolase], reverse protein ADP-ribosylation. In the present study, we show that human Nudix (nucleoside diphosphate-linked moiety X)-type motif 16 (hNUDT16) represents a new enzyme class that can process protein ADP-ribosylation in vitro, converting it into ribose-5'-phosphate (R5P) tags covalently attached to the modified proteins. Furthermore, our data show that hNUDT16 enzymatic activity can be used to trim ADP-ribosylation on proteins in order to facilitate analysis of ADP-ribosylation sites on proteins by MS.
Databáze: MEDLINE