HSP70 binds to specific non-coding RNA and regulates human RNA polymerase III
OPEN ACCESS
Loading...
Author / Producer
Date
2024-02-15
Publication Type
Journal Article
ETH Bibliography
yes
Citations
Altmetric
OPEN ACCESS
Data
Rights / License
Abstract
Molecular chaperones are critical for protein homeostasis and are implicated in several human pathologies such as neurodegeneration and cancer. While the binding of chaperones to nascent and misfolded proteins has been studied in great detail, the direct interaction between chaperones and RNA has not been systematically investigated. Here, we provide the evidence for widespread interaction between chaperones and RNA in human cells. We show that the major chaperone heat shock protein 70 (HSP70) binds to non -coding RNA transcribed by RNA polymerase III (RNA Pol III) such as tRNA and 5S rRNA. Global chromatin profiling revealed that HSP70 binds genomic sites of transcription by RNA Pol III. Detailed biochemical analyses showed that HSP70 alleviates the inhibitory effect of cognate tRNA transcript on tRNA gene transcription. Thus, our study uncovers an unexpected role of HSP70-RNA interaction in the biogenesis of a specific class of non -coding RNA with wider implications in cancer therapeutics.
Permanent link
Publication status
published
External links
Editor
Book title
Journal / series
Volume
84 (4)
Pages / Article No.
687 - 7010000000
Publisher
Cell Press
Event
Edition / version
Methods
Software
Geographic location
Date collected
Date created
Subject
molecular chaperones; HSP70; RNA-binding proteome; RNA polymerase III; tRNA; proteostasis; non-coding RNA; heat-shock proteins; transcription; RNA-protein interaction