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

ABSTRACT: ADPr sites on histones obtained from cells were directly identified. 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.

INSTRUMENT(S): Orbitrap Fusion ETD

ORGANISM(S): Homo Sapiens (human) Gallus Gallus (chicken)

TISSUE(S): Cell Culture

SUBMITTER: Thomas Colby

LAB HEAD: Ivan Matic

PROVIDER: PXD005462 | Pride | 2016-12-22

REPOSITORIES: Pride

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Dataset's files

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			Action	DRS
	160121_FS1_DT40_H2O2_Core_ETD.raw	Raw
	160129_FS1_U2OS_H2O2_H1_ETD_Rep1.raw	Raw
	160129_FS1_U2OS_H2O2_H1_ETD_Rep2.raw	Raw
	160204_FS1_U2OS_H2O2_Core_IMAC_ETD_Rep1.raw	Raw
	160205_FS1_U2OS_H2O2_Core_IMAC_ETD_Rep2.raw	Raw

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Publications

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]

PMID: 27723750

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Affinity purification of ADP-ribosylated proteins from A. thaliana plants expressing the Pseudomonas syringae type III effector AvrRpm1 (2.5 ug Af1521 Macro, technical replicate 1)

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