Chemical genetic discovery of PARP targets reveals a role for PARP-1 in transcription elongation
Author(s) -
Bryan A. Gibson,
Yajie Zhang,
Hong Jiang,
Kristine M. Hussey,
Jonathan H. Shrimp,
Hening Lin,
Frank Schwede,
Yonghao Yu,
W. Lee Kraus
Publication year - 2016
Publication title -
science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 12.556
H-Index - 1186
eISSN - 1095-9203
pISSN - 0036-8075
DOI - 10.1126/science.aaf7865
Subject(s) - nad+ kinase , poly adp ribose polymerase , adp ribosylation , nicotinamide adenine dinucleotide , polymerase , rna polymerase ii , biology , proteome , biochemistry , chemistry , microbiology and biotechnology , enzyme , promoter , gene expression , gene
Mapping ADP-ribosylation by PARPs During many cell processes, ADP-ribose is transferred from NAD+ onto protein substrates by poly(ADP-ribose) polymerases (PARPs). Gibsonet al. developed a method to track ribose transfer events and mapped hundreds of sites of ADP-ribosylation for PARPs 1, 2, and 3 across the proteome and genome. One PARP-1 target is NELF, a protein complex that regulates pausing by RNA polymerase II. If NELF is ribosylated, pausing is released and productive transcription elongation resumes.Science , this issue p.45
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