Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Insight into the RssB-Mediated Recognition and Delivery of σs to the AAA+ Protease, ClpXP.

Biomolecules - 16 Apr 2020

Micevski Dimce, Zeth Kornelius, Mulhern Terrence D, Schuenemann Verena J, Zammit Jessica E, Truscott Kaye N, Dougan David A

Abstract excerpt

In Escherichia coli, SigmaS (σS) is the master regulator of the general stress response. The cellular levels of σS are controlled by transcription, translation and protein stability. The turnover of σS, by the AAA+ protease (ClpXP), is tightly regulated by a dedicated adaptor protein, termed RssB (Regulator of Sigma S protein B)-which is an atypical member of the response regulator (RR) family. Currently however,...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to ATPases Associated with Diverse Cellular Activities
Share to Endopeptidase Clp

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Escherichia coli Proteins

Share to Molecular Chaperones

Share to Protein Domains

Share to Scattering, Small Angle

Share to Sigma Factor

Share to X-Ray Diffraction

Source

Open in PubMed Open full text

Identifiers

PMID: 32316259
DOI: 10.3390/biom10040615
PMCID: PMC7226468

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Insight into the RssB-Mediated Recognition and Delivery of σs to the AAA+ Protease, ClpXP.PMID 32316259Read ↗

Role of the response regulator RssB in sigma recognition and initiation of sigma proteolysis in Escherichia coli.Semantic proximity Read ↗

The response regulator RssB, a recognition factor for sigmaS proteolysis in Escherichia coli, can act like an anti-sigmaS factor.Semantic proximity Read ↗

Anti-adaptors provide multiple modes for regulation of the RssB adaptor protein.Semantic proximity Read ↗

Flexible linkers leash the substrate binding domain of SspB to a peptide module that stabilizes delivery complexes with the AAA+ ClpXP protease.Semantic proximity Read ↗

Functional and structural characterization of RsbU, a stress signaling protein phosphatase 2C.Semantic proximity Read ↗

Listeria monocytogenes Requires the RsbX Protein To Prevent SigB Activation under Nonstressed Conditions.Semantic proximity Read ↗

Versatile modes of peptide recognition by the ClpX N domain mediate alternative adaptor-binding specificities in different bacterial species.Semantic proximity Read ↗

Structural and functional characterization of partner switching regulating the environmental stress response in Bacillus subtilis.Semantic proximity Read ↗

Arginine phosphorylation marks proteins for degradation by a Clp protease.Semantic proximity Read ↗

A specificity-enhancing factor for the ClpXP degradation machine.Semantic proximity Read ↗

Roles of individual domains and conserved motifs of the AAA+ chaperone ClpB in oligomerization, ATP hydrolysis, and chaperone activity.Semantic proximity Read ↗

A two-component phosphotransfer network involving ArcB, ArcA, and RssB coordinates synthesis and proteolysis of sigmaS (RpoS) in E. coli.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.