ArticlePloS one2014
Interaction of a partially disordered antisigma factor with its partner, the signaling domain of the TonB-dependent transporter HasR.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 13 citations in OpenAlex.
- A generalizable method for the purification and biophysical characterization of bacterial membrane receptors.Protein science : a publication of the Protein Society · 2026Article
- Structural Analysis of Proteins from Bacterial Secretion Systems and Their Assemblies by NMR Spectroscopy.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Transcription regulation of iron carrier transport genes by ECF sigma factors through signaling from the cell surface into the cytoplasm.FEMS microbiology reviews · 2022Article
- Insights into SusCD-mediated glycan import by a prominent gut symbiont.Nature communications · 2021Article
- Extracellular haem utilization by the opportunistic pathogen Pseudomonas aeruginosa and its role in virulence and pathogenesis.Advances in microbial physiology · 2021Article
- Structural basis of cell-surface signaling by a conserved sigma regulator in Gram-negative bacteria.The Journal of biological chemistry · 2020Article
- Structural basis of the signalling through a bacterial membrane receptor HasR deciphered by an integrative approach.The Biochemical journal · 2016Article
- Mechanistic Implications of the Unique Structural Features and Dimerization of the Cytoplasmic Domain of the Pseudomonas Sigma Regulator, PupR.Biochemistry · 2015Article
- Self-cleavage of the Pseudomonas aeruginosa Cell-surface Signaling Anti-sigma Factor FoxR Occurs through an N-O Acyl Rearrangement.The Journal of biological chemistry · 2015Article
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Authors and funding
12 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bacteria use diverse signaling pathways to control gene expression in response to external stimuli. In Gram-negative bacteria, the binding of a nutrient is sensed by an outer membrane transporter. This signal is then transmitted to an antisigma factor and subsequently to the cytoplasm where an ECF sigma factor induces expression of genes related to the acquisition of this nutrient. The molecular interactions involved in this transmembrane signaling are poorly understood and structural data on this family of antisigma factor are rare. Here, we present the first structural study of the periplasmic domain of an antisigma factor and its interaction with the transporter. The study concerns the signaling in the heme acquisition system (Has) of Serratia marcescens. Our data support unprecedented partially disordered periplasmic domain of an anti-sigma factor HasS in contact with a membrane-mimicking environment. We solved the 3D structure of the signaling domain of HasR transporter and identified the residues at the HasS-HasR interface. Their conservation in several bacteria suggests wider significance of the proposed model for the understanding of bacterial transmembrane signaling.
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