Serine is a new target residue for endogenous ADP-ribosylation on histones

被引:187
作者
Leidecker, Orsolya [1 ]
Bonfiglio, Juan Jose [1 ]
Colby, Thomas [1 ]
Zhang, Qi [1 ]
Atanassov, Ilian [1 ]
Zaja, Roko [2 ]
Palazzo, Luca [2 ]
Stockum, Anna [1 ]
Ahel, Ivan [2 ]
Matic, Ivan [1 ]
机构
[1] Max Planck Inst Biol Ageing, Cologne, Germany
[2] Univ Oxford, Sir William Dunn Sch Pathol, Oxford, England
基金
英国惠康基金; 欧洲研究理事会;
关键词
NUDIX HYDROLASES; IDENTIFICATION; PROTEOMICS; CHROMATIN; RIBOSE; SITES; CELLS;
D O I
10.1038/nchembio.2180
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
ADP-ribosylation (ADPr) is a biologically and clinically important post-translational modification, but little is known about the amino acids it targets on cellular proteins. Here we present a proteomic approach for direct in vivo identification and quantification of ADPr sites on histones. We have identified 12 unique ADPr sites in human osteosarcoma cells and report serine ADPr as a new type of histone mark that responds to DNA damage.
引用
收藏
页码:998 / +
页数:6
相关论文
共 28 条
[1]   Immunodot blot method for the detection of poly(ADP-ribose) synthesized in vitro and in vivo [J].
Affar, EB ;
Duriez, PJ ;
Shah, RG ;
Sallmann, FR ;
Bourassa, S ;
Küpper, JH ;
Bürkle, A ;
Poirier, GG .
ANALYTICAL BIOCHEMISTRY, 1998, 259 (02) :280-283
[2]   The Promise of Proteomics for the Study of ADP-Ribosylation [J].
Bock, Florian J. ;
Todorova, Tanya T. ;
Chang, Paul .
MOLECULAR CELL, 2015, 58 (06) :911-924
[3]   PROTEIN MODIFICATION BY ADP-RIBOSE VIA ACID-LABILE LINKAGES [J].
CERVANTESLAUREAN, D ;
LOFLIN, PT ;
MINTER, DE ;
JACOBSON, EL ;
JACOBSON, MK .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1995, 270 (14) :7929-7936
[4]   Andromeda: A Peptide Search Engine Integrated into the MaxQuant Environment [J].
Cox, Juergen ;
Neuhauser, Nadin ;
Michalski, Annette ;
Scheltema, Richard A. ;
Olsen, Jesper V. ;
Mann, Matthias .
JOURNAL OF PROTEOME RESEARCH, 2011, 10 (04) :1794-1805
[5]   MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification [J].
Cox, Juergen ;
Mann, Matthias .
NATURE BIOTECHNOLOGY, 2008, 26 (12) :1367-1372
[6]   Poly(ADP-ribosyl)ation reactions in the regulation of nuclear functions [J].
D'Amours, D ;
Desnoyers, S ;
D'Silva, I ;
Poirier, GG .
BIOCHEMICAL JOURNAL, 1999, 342 :249-268
[7]   Nudix hydrolases degrade protein-conjugated ADP-ribose [J].
Daniels, Casey M. ;
Thirawatananond, Puchong ;
Ong, Shao-En ;
Gabelli, Sandra B. ;
Leung, Anthony K. L. .
SCIENTIFIC REPORTS, 2015, 5
[8]   Phosphoproteomic Approach to Characterize Protein Mono- and Poly(ADP-ribosyl)ation Sites from Cells [J].
Daniels, Casey M. ;
Ong, Shao-En ;
Leung, Anthony K. L. .
JOURNAL OF PROTEOME RESEARCH, 2014, 13 (08) :3510-3522
[9]   Chromatin to Clinic: The Molecular Rationale for PARP1 Inhibitor Function [J].
Feng, Felix Y. ;
De Bono, Johann S. ;
Rubin, Mark A. ;
Knudsen, Karen E. .
MOLECULAR CELL, 2015, 58 (06) :925-934
[10]   A review of tandem mass spectrometry characterization of adenosine diphosphate-ribosylated peptides [J].
Hengel, Shawna M. ;
Goodlett, David R. .
INTERNATIONAL JOURNAL OF MASS SPECTROMETRY, 2012, 312 :114-121