ArticleJournal of bacteriology2006
A caulobacter crescentus extracytoplasmic function sigma factor mediating the response to oxidative stress in stationary phase.
Article in Journal of bacteriology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed.
- A calcium-binding protein-sigV regulatory circuit modulates stress adaptation and persistence in Caulobacter vibrioides.Archives of microbiology · 2026Article
- Biosynthesis of Peptidic Thiooxazole Metallophores Installed by Multinuclear Nonheme Iron Enzymes.ACS chemical biology · 2026Article
- Biosynthesis of peptidic thiooxazole metallophores installed by multinuclear nonheme iron enzymes.bioRxiv : the preprint server for biology · 2025Article
- A widespread family of ribosomal peptide metallophores involved in bacterial adaptation to metal stress.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- The ChvG-ChvI and NtrY-NtrX Two-Component Systems Coordinately Regulate Growth of Caulobacter crescentus.Journal of bacteriology · 2021Article
- Environmental Conditions Modulate the Transcriptomic Response of BothMicroorganisms · 2021Article
- An Extracytoplasmic Function Sigma/Anti-Sigma Factor System Regulates Hypochlorous Acid Resistance and Impacts Expression of the Type IV Secretion System inJournal of bacteriology · 2021Article
- Article
- MostmSphere · 2018Article
- Regulated Proteolysis in Bacteria: Caulobacter.Annual review of genetics · 2016Review
- Transcriptomic analysis of the stationary phase response regulator SpdR in Caulobacter crescentus.BMC microbiology · 2016Article
- Response of single bacterial cells to stress gives rise to complex history dependence at the population level.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- The Caulobacter crescentus Homolog of DnaA (HdaA) Also Regulates the Proteolysis of the Replication Initiator Protein DnaA.Journal of bacteriology · 2015Article
- Article
- Decreased in vivo virulence and altered gene expression by a Brucella melitensis light-sensing histidine kinase mutant.Pathogens and disease · 2015Article
- General Stress Signaling in the Alphaproteobacteria.Annual review of genetics · 2015Review
- Article
- Gene expression and physiological role of Pseudomonas aeruginosa methionine sulfoxide reductases during oxidative stress.Journal of bacteriology · 2013Article
- The extracytoplasmic function sigma factor EcfO protects Bacteroides fragilis against oxidative stress.Journal of bacteriology · 2013Article
- Extracytoplasmic function (ECF) sigma factor σF is involved in Caulobacter crescentus response to heavy metal stress.BMC microbiology · 2012Article
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Alternative sigma factors of the extracytoplasmic function (ECF) subfamily are important regulators of stress responses in bacteria and have been implicated in the control of homeostasis of the extracytoplasmic compartment of the cell. This work describes the characterization of sigF, encoding 1 of the 13 members of this subfamily identified in Caulobacter crescentus. A sigF-null strain was obtained and shown to be severely impaired in resistance to oxidative stress, caused by hydrogen peroxide treatment, exclusively during the stationary phase. Although sigF mRNA levels decrease in stationary-phase cells, the amount of sigma(F) protein is greatly increased at this stage, indicating a posttranscriptional control. Data obtained indicate that the FtsH protease is either directly or indirectly involved in the control of sigma(F) levels, as cells lacking this enzyme present larger amounts of the sigma factor. Increased stability of sigma(F) protein in stationary-phase cells of the parental strain and in exponential-phase cells of the ftsH-null strain is also demonstrated. Transcriptome analysis of the sigF-null strain led to the identification of eight genes regulated by sigma(F) during the stationary phase, including sodA and msrA, which are known to be involved in oxidative stress response.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.