ArticleJournal of bacteriology2007
Mapping critical interactive sites within the periplasmic domain of the Vibrio cholerae type II secretion protein EpsM.
Article in Journal of bacteriology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 28 citations in OpenAlex.
- The PDZ domain of EpsC is required for extracellular secretion of VesB by the Type II secretion system inJournal of bacteriology · 2025Article
- In situ structure of a bacterial flagellar motor at subnanometre resolution reveals adaptations for increased torque.Nature microbiology · 2025Article
- Molecular model of a bacterial flagellar motorbioRxiv : the preprint server for biology · 2024Article
- ClpA affects the virulence ofFrontiers in microbiology · 2024Article
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- Article
- Functional and structural characterization of Vibrio cholerae extracellular serine protease B, VesB.The Journal of biological chemistry · 2014Article
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- Dynamic interplay between the periplasmic and transmembrane domains of GspL and GspM in the type II secretion system.PloS one · 2013Article
- Functional characterization of EpsC, a component of the type II secretion system, in the pathogenicity of Vibrio vulnificus.Infection and immunity · 2011Article
- Proteomic analysis of the Vibrio cholerae type II secretome reveals new proteins, including three related serine proteases.The Journal of biological chemistry · 2011Article
- Oligomerization of EpsE coordinates residues from multiple subunits to facilitate ATPase activity.The Journal of biological chemistry · 2011Article
- In vivo cross-linking of EpsG to EpsL suggests a role for EpsL as an ATPase-pseudopilin coupling protein in the Type II secretion system of Vibrio cholerae.Molecular microbiology · 2011Article
- The dimer formed by the periplasmic domain of EpsL from the Type 2 Secretion System of Vibrio parahaemolyticus.Journal of structural biology · 2009Article
- The three-dimensional structure of the cytoplasmic domains of EpsF from the type 2 secretion system of Vibrio cholerae.Journal of structural biology · 2009Article
- Docking and assembly of the type II secretion complex of Vibrio cholerae.Journal of bacteriology · 2009Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The type II secretion (T2S) system is present in many gram-negative species, both pathogenic and nonpathogenic, where it supports the delivery of a variety of toxins, proteases, and lipases into the extracellular environment. In Vibrio cholerae, the T2S apparatus is composed of 12 Eps proteins that assemble into a multiprotein complex that spans the entire cell envelope. Two of these proteins, EpsM and EpsL, are key components of the secretion machinery present in the inner membrane. In addition to likely forming homodimers, EpsL and EpsM have been shown to form a stable complex in the inner membrane and to protect each other from proteolytic degradation. To identify and map the specific regions of EpsM involved in protein-protein interactions with both another molecule of EpsM and EpsL, we tested the interactions of deletion constructs of EpsM with full-length EpsM and EpsL by functional characterization and copurification as well as coimmunoprecipitation. Analysis of the truncated EpsM mutants revealed that the region of EpsM from amino acids 100 to 135 is necessary for EpsM to form homo-oligomers, while residues 84 to 99 appear to be critical for a stable interaction with EpsL.
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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.