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Heat-shock protein 90 globally targets paused promoters and regulates environment-induced gene expression

ABSTRACT: In this study we provide evidence that Hsp90 binds chromatin at specific sites close to several TSS in Drosophila S2 cell line. In addition of finding a preference for stalled promoter regions of annotated genes, we uncover many intergenic Hsp90 binding sites coinciding with non-annotated transcription start sites. Interestingly, this set includes promoters for primary transcripts of microRNA genes, thereby expanding the scope of Hsp90 to transcriptional control of many genes. We finally conclude that Hsp90 contacts NelfE and thus regulates pol II pausing. Our Dataset comprises of 1 ChIP-seq sample using chromatin from S2 cells which was immunoprecipitated, using antibodies against Drosophila Hsp90. The two biological replicates are submitted along with the input replicates.

ORGANISM(S): Drosophila melanogaster

SUBMITTER: Cem Sievers

PROVIDER: E-GEOD-31226 | biostudies-arrayexpress |

REPOSITORIES: biostudies-arrayexpress

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Hsp90 globally targets paused RNA polymerase to regulate gene expression in response to environmental stimuli.

Sawarkar Ritwick R Sievers Cem C Paro Renato R

Cell 20120501 4

The molecular chaperone Heat shock protein 90 (Hsp90) promotes the maturation of several important proteins and plays a key role in development, cancer progression, and evolutionary diversification. By mapping chromatin-binding sites of Hsp90 at high resolution across the Drosophila genome, we uncover an unexpected mechanism by which Hsp90 orchestrates cellular physiology. It localizes near promoters of many coding and noncoding genes including microRNAs. Using computational and biochemical anal ...[more]

PMID: 22579285

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