z-logo
open-access-imgOpen Access
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

The content you want is available to Zendy users.

Already have an account? Click here to sign in.
Having issues? You can contact us here
Accelerating Research

Address

John Eccles House
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom