ArticleFEMS microbiology letters2014
Interplay among Pseudomonas syringae HrpR, HrpS and HrpV proteins for regulation of the type III secretion system.
Article in FEMS microbiology letters, 2014. 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, 24 citations in OpenAlex.
- Novel insights into the genetic basis and transcriptomic elucidation of virulence attenuation inVirulence · 2025Article
- VimR is a conserved master transcription regulator controlling virulence and metabolism in Pseudomonas.Nucleic acids research · 2025Article
- The RNA repair proteins RtcAB regulate transcription activator RtcR via its CRISPR-associated Rossmann fold domain.iScience · 2022Article
- The OmpR-like Transcription Factor as a Negative Regulator ofInternational journal of molecular sciences · 2022Article
- Interactions between paralogous bacterial enhancer-binding proteins enable metal-dependent regulation of alternative nitrogenases in Azotobacter vinelandii.Molecular microbiology · 2022Article
- Regulation of theMicroorganisms · 2021Review
- Pseudomonas syringae AlgU Downregulates Flagellin Gene Expression, Helping Evade Plant Immunity.Journal of bacteriology · 2020Article
- Mechanisms of σJournal of molecular biology · 2019Review
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- Article
- The pathogenicity factor HrpF interacts with HrpA and HrpG to modulate type III secretion system (T3SS) function and t3ss expression in Pseudomonas syringae pv. averrhoi.Molecular plant pathology · 2016Article
- In depth analysis of the mechanism of action of metal-dependent sigma factors: characterization of CorE2 from Myxococcus xanthus.Nucleic acids research · 2016Article
- Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Pseudomonas syringae pv. tomato DC3000, a plant pathogenic gram-negative bacterium, employs the type III secretion system (T3SS) to cause disease in tomato and Arabidopsis and to induce the hypersensitive response in nonhost plants. The expression of T3SS is regulated by the HrpL extracytoplasmic sigma factor. Expression of HrpL is controlled by transcriptional activators HrpR and HrpS and negative regulator HrpV. In this study, we analysed the organization of HrpRS and HrpV regulatory proteins and interplay between them. We identified one key residue I26 in HrpS required for repression by HrpV. Substitution of I26 in HrpS abolishes its interaction with HrpV and impairs interactions between HrpS and HrpR and the self-association of HrpS. We show that HrpS self-associates and can associate simultaneously with HrpR and HrpV. We now propose that HrpS has a central role in the assembly of the regulatory HrpRSV complex. Deletion analysis of HrpR and HrpS proteins showed that C-terminal parts of HrpR and HrpS confer determinants indispensable for their self-assembly.
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