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


ABSTRACT: 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.

SUBMITTER: Leidecker O 

PROVIDER: S-EPMC5113755 | biostudies-literature | 2016 Dec

REPOSITORIES: biostudies-literature

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

Leidecker Orsolya O   Bonfiglio Juan José JJ   Colby Thomas T   Zhang Qi Q   Atanassov Ilian I   Zaja Roko R   Palazzo Luca L   Stockum Anna A   Ahel Ivan I   Matic Ivan I  

Nature chemical biology 20161010 12


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. ...[more]

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