ArticleProceedings of the National Academy of Sciences of the United States of America2006
Disulfide cross-linking indicates that FlgM-bound and free sigma28 adopt similar conformations.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 23 citations in OpenAlex.
- c-di-GMP Arms an Anti-σ to Control Progression of Multicellular Differentiation in Streptomyces.Molecular cell · 2020Article
- Structural basis for transcription activation by Crl through tethering of σProceedings of the National Academy of Sciences of the United States of America · 2019Article
- Crystal structure ofProceedings of the National Academy of Sciences of the United States of America · 2017Article
- Binding interface between the Salmonella σ(S)/RpoS subunit of RNA polymerase and Crl: hints from bacterial species lacking crl.Scientific reports · 2015Article
- DNA-binding properties of the Bacillus subtilis and Aeribacillus pallidus AC6 σ(D) proteins.Journal of bacteriology · 2011Article
- Identification of conserved amino acid residues of the Salmonella sigmaS chaperone Crl involved in Crl-sigmaS interactions.Journal of bacteriology · 2010Article
- Reduced capacity of alternative sigmas to melt promoters ensures stringent promoter recognition.Genes & development · 2009Article
- Mutational analysis of Escherichia coli sigma28 and its target promoters reveals recognition of a composite -10 region, comprised of an 'extended -10' motif and a core -10 element.Molecular microbiology · 2009Article
- Mutagenesis of region 4 of sigma 28 from Chlamydia trachomatis defines determinants for protein-protein and protein-DNA interactions.Journal of bacteriology · 2009Article
- Binding of the unorthodox transcription activator, Crl, to the components of the transcription machinery.The Journal of biological chemistry · 2008Article
- A full-length group 1 bacterial sigma factor adopts a compact structure incompatible with DNA binding.Chemistry & biology · 2008Article
- Regulation of bacterial RNA polymerase sigma factor activity: a structural perspective.Current opinion in microbiology · 2008Review
- Rapid microwave-assisted CNBr cleavage of bead-bound peptides.Journal of combinatorial chemistryArticle
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
The dissociable sigma subunit of bacterial RNA polymerase is required for the promoter-specific initiation of transcription. When bound to RNA polymerase, sigma makes sequence-specific promoter contacts and plays a crucial role in DNA melting. In isolation, however, sigma lacks significant promoter binding activity. In the crystal structure of the flagellar sigma factor, sigma(28), bound to the anti-sigma factor, FlgM, sigma(28) adopts a compact conformation in which the promoter binding surfaces are occluded by interdomain contacts. To test whether sigma(28) adopts this conformation in the absence of FlgM, we engineered a set of double cysteine mutants predicted to form interdomain disulfides in the conformation observed in the FlgM complex. We show that these disulfides form in both the presence and absence of FlgM. For two of the mutants, quantitative measurements of disulfide formation under equilibrium conditions suggest that the major solution conformation favors disulfide formation. The results indicate that the compact conformation of sigma(28) observed in the sigma(28)/FlgM structure is similar to the predominant conformation of free sigma(28) in solution. This finding suggests that autoinhibition of DNA binding in free sigma(28) is accomplished by steric occlusion of the promoter binding surfaces by interdomain interactions within the sigma factor as well as by a suboptimal distance between the promoter -10 and -35 element binding determinants in sigma(2) and sigma(4), respectively.
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