Mass spectrometry for serine ADP-ribosylation? Think o-glycosylation!

被引：36

作者：

Bonfiglio, Juan J. ^{[1
]}

Colby, Thomas ^{[1
]}

Matic, Ivan ^{[1
]}

机构：

[1] Max Planck Inst Biol Ageing, Joseph Stelzmann Str 9B, D-50931 Cologne, Germany

来源：

NUCLEIC ACIDS RESEARCH | 2017年 / 45卷 / 11期

关键词：

RIBOSE ACCEPTOR SITES; DISSOCIATION FRAGMENTATION; NUDIX HYDROLASES; LYSINE RESIDUES; PROTEIN; IDENTIFICATION; PEPTIDE; CELLS; PARP1; POLY(ADP-RIBOSYL)ATION;

D O I：

10.1093/nar/gkx446

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：

Protein ADP-ribosylation (ADPr), a biologically and clinically important post-translational modification, exerts its functions by targeting a variety of different amino acids. Its repertoire recently expanded to include serine ADPr, which is emerging as an important and widespread signal in the DNA damage response. Chemically, serine ADPr (andmore generally o-glycosidic ADPr) is a form of o-glycosylation, and its extreme lability renders it practically invisible to standard mass spectrometry approaches, often leading to erroneous localizations. The knowledge from the mature field of o-glycosation and our own initial difficulties with mass spectrometric analyzes of serine ADPr suggest how to avoid these misidentifications and fully explore the scope of o-glycosidic ADPr in DNA damage response and beyond.

引用

页码：6259 / 6264

页数：6

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