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Title: A Novel SRP Recognition Sequence in the Homeostatic Control Region of Heat Shock Transcription Factor σ[32].
Authors: Miyazaki, Ryoji
Yura, Takashi
Suzuki, Takehiro
Dohmae, Naoshi
Mori, Hiroyuki  kyouindb  KAKEN_id  orcid (unconfirmed)
Akiyama, Yoshinori  kyouindb  KAKEN_id  orcid (unconfirmed)
Author's alias: 森, 博幸
秋山, 芳展
Issue Date: 7-Apr-2016
Publisher: Nature Publishing Group
Journal title: Scientific reports
Volume: 6
Thesis number: 24147
Abstract: Heat shock response (HSR) generally plays a major role in sustaining protein homeostasis. In Escherichia coli, the activity and amount of the dedicated transcription factor σ[32] transiently increase upon heat shock. The initial induction is followed by chaperone-mediated negative feedback to inactivate and degrade σ[32]. Previous work reported that signal recognition particle (SRP)-dependent targeting of σ[32] to the membrane is essential for feedback control, though how SRP recognizes σ[32] remained unknown. Extensive photo- and disulfide cross-linking studies in vivo now reveal that the highly conserved regulatory region of σ[32] that lacks a consecutive hydrophobic stretch interacts with the signal peptide-binding site of Ffh (the protein subunit of SRP). Importantly, the σ[32]–Ffh interaction observed was significantly affected by mutations in this region that compromise the feedback regulation, but not by deleting the DnaK/DnaJ chaperones. Homeostatic regulation of HSR thus requires a novel type of SRP recognition mechanism.
Rights: This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article's Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit
DOI(Published Version): 10.1038/srep24147
PubMed ID: 27052372
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