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PARP‐1 transcriptional activity is regulated by sumoylation upon heat shock
Author(s) -
Martin Nadine,
Schwamborn Klaus,
Schreiber Valérie,
Werner Andreas,
Guillier Christelle,
Zhang XiangDong,
Bischof Oliver,
Seeler JacobS,
Dejean Anne
Publication year - 2009
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1038/emboj.2009.279
Subject(s) - sumo protein , biology , rnf4 , hsp70 , ubiquitin ligase , microbiology and biotechnology , chromatin immunoprecipitation , ubiquitin , heat shock protein , poly adp ribose polymerase , transcription (linguistics) , heat shock , gene expression , transcription factor , gene , promoter , polymerase , genetics , zinc finger , linguistics , philosophy
Heat shock and other environmental stresses rapidly induce transcriptional responses subject to regulation by a variety of post‐translational modifications. Among these, poly(ADP‐ribosyl)ation and sumoylation have received growing attention. Here we show that the SUMO E3 ligase PIASy interacts with the poly(ADP‐ribose) polymerase PARP‐1, and that PIASy mediates heat shock‐induced poly‐sumoylation of PARP‐1. Furthermore, PIASy, and hence sumoylation, appears indispensable for full activation of the inducible HSP70.1 gene. Chromatin immunoprecipitation experiments show that PIASy, SUMO and the SUMO‐conjugating enzyme Ubc9 are rapidly recruited to the HSP70.1 promoter upon heat shock, and that they are subsequently released with kinetics similar to PARP‐1. Finally, we provide evidence that the SUMO‐targeted ubiquitin ligase RNF4 mediates heat‐shock‐inducible ubiquitination of PARP‐1, regulates the stability of PARP‐1, and, like PIASy, is a positive regulator of HSP70.1 gene activity. These results, thus, point to a novel mechanism for regulating PARP‐1 transcription function, and suggest crosstalk between sumoylation and RNF4‐mediated ubiquitination in regulating gene expression in response to heat shock.