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2017 ; 65
(5
): 932-940.e6
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Serine ADP-Ribosylation Depends on HPF1
#MMPMID28190768
Bonfiglio JJ
; Fontana P
; Zhang Q
; Colby T
; Gibbs-Seymour I
; Atanassov I
; Bartlett E
; Zaja R
; Ahel I
; Matic I
Mol Cell
2017[Mar]; 65
(5
): 932-940.e6
PMID28190768
show ga
ADP-ribosylation (ADPr) regulates important patho-physiological processes through
its attachment to different amino acids in proteins. Recently, by precision
mapping on all possible amino acid residues, we identified histone serine ADPr
marks in the DNA damage response. However, the biochemical basis underlying this
serine modification remained unknown. Here we report that serine ADPr is strictly
dependent on histone PARylation factor 1 (HPF1), a recently identified regulator
of PARP-1. Quantitative proteomics revealed that serine ADPr does not occur in
cells lacking HPF1. Moreover, adding HPF1 to in vitro PARP-1/PARP-2 reactions is
necessary and sufficient for serine-specific ADPr of histones and PARP-1 itself.
Three endogenous serine ADPr sites are located on the PARP-1 automodification
domain. Further identification of serine ADPr on HMG proteins and hundreds of
other targets indicates that serine ADPr is a widespread modification. We propose
that O-linked protein ADPr is the key signal in PARP-1/PARP-2-dependent processes
that govern genome stability.
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