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

The Spo0A sof mutations reveal regions of the regulatory domain that interact with a sensor kinase and RNA polymerase.

Molecular microbiology - 1 Jan 1999

Cervin M A, Spiegelman G B

Abstract excerpt

Spo0A is a two-domain response regulator required for the initiation of sporulation in Bacillus subtilis. Spo0A is activated by phosphorylation of its regulatory domain by a multicomponent phosphorelay. To define the role of the regulatory domain in the activation of Spo0A, we have characterized four of the sof mutations in vitro. The sof mutations were identified previously as suppressors of the...

Read the complete abstract on PubMed

Topics

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

Share to Bacillus subtilis
Share to Binding Sites
Share to DNA-Directed RNA Polymerases

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Phosphoric Monoester Hydrolases

Share to Phosphorylation

Share to Protein Kinases

Share to Sigma Factor

Share to Transcription, Genetic

Source

Identifiers

PMID: 10027976
DOI: 10.1046/j.1365-2958.1999.01200.x

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The Spo0A sof mutations reveal regions of the regulatory domain that interact with a sensor kinase and RNA polymerase.PMID 10027976Read ↗

Structural alterations in the Bacillus subtilis Spo0A regulatory protein which suppress mutations at several spo0 loci.Semantic proximity Read ↗

Spo0A activates and represses its own synthesis by binding at its dual promoters.Semantic proximity Read ↗

Novel mutations that alter the regulation of sporulation in Bacillus subtilis. Evidence that phosphorylation of regulatory protein SpoOA controls the initiation of sporulation.Semantic proximity Read ↗

Multiple histidine kinases regulate entry into stationary phase and sporulation in Bacillus subtilis.Semantic proximity Read ↗

Spo0A mutants of Bacillus subtilis with sigma factor-specific defects in transcription activation.Semantic proximity Read ↗

Interaction surface of the Spo0A response regulator with the Spo0E phosphatase.Semantic proximity Read ↗

Dimer form of phosphorylated Spo0A, a transcriptional regulator, stimulates the spo0F transcription at the initiation of sporulation in Bacillus subtilis.Semantic proximity Read ↗

A genetic analysis of Spo0A structure and function.Semantic proximity Read ↗

Multiple protein-aspartate phosphatases provide a mechanism for the integration of diverse signals in the control of development in B. subtilis.Semantic proximity Read ↗

Mutational dissociation of the positive and negative regulatory properties of the Spo0A sporulation transcription factor of Bacillus subtilis.Semantic proximity Read ↗

SpoIIE governs the phosphorylation state of a protein regulating transcription factor sigma F during sporulation in Bacillus subtilis.Semantic proximity Read ↗

Crystal structure of a phosphatase-resistant mutant of sporulation response regulator Spo0F from Bacillus subtilis.Semantic proximity Read ↗

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