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.
Serine is a new target residue for endogenous ADP-ribosylation on histones / Leidecker, O; Bonfiglio, Jj; Colby, T; Zhang, Q; Atanassov, I; Zaja, R; Palazzo, L; Stockum, A; Ahel, I; Matic, I.. - In: NATURE CHEMICAL BIOLOGY. - ISSN 1552-4450. - (2016). [10.1038/nchembio.2180]
Serine is a new target residue for endogenous ADP-ribosylation on histones
Palazzo L;
2016
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.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
