ArticlePloS one2012
HrcQ provides a docking site for early and late type III secretion substrates from Xanthomonas.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 33 citations in OpenAlex.
- Type III secretion system chaperones: a helping hand for secretion.Microbiology (Reading, England) · 2026Review
- The predicted sorting platform dynamically associates with the type III secretion system from Xanthomonas euvesicatoria in response to the external pH.BMC microbiology · 2025Article
- On the role of the sorting platform in hierarchical type III secretion regulation in enteropathogenicJournal of bacteriology · 2025Article
- Transcriptomic data reveals an auxiliary detoxification mechanism that alleviates formaldehyde stress in Methylobacterium sp. XJLW.BMC genomics · 2024Article
- Article
- Functional characterization of VirB/VirD4 and Icm/Dot type IV secretion systems from the plant-pathogenic bacteriumFrontiers in cellular and infection microbiology · 2023Article
- Recognition of a translocation motif in the regulator HpaA fromFrontiers in plant science · 2022Article
- Article
- The Contribution of the Predicted Sorting Platform Component HrcQ to Type III Secretion inFrontiers in microbiology · 2021Article
- A conserved motif promotes HpaB-regulated export of type III effectors from Xanthomonas.Molecular plant pathology · 2018Article
- A 1-phytase type III effector interferes with plant hormone signaling.Nature communications · 2017Article
- Identification of new protein-coding genes with a potential role in the virulence of the plant pathogen Xanthomonas euvesicatoria.BMC genomics · 2017Article
- The Predicted Lytic Transglycosylase HpaH from Xanthomonas campestris pv. vesicatoria Associates with the Type III Secretion System and Promotes Effector Protein Translocation.Infection and immunity · 2017Article
- The TAL Effector AvrBs3 fromFrontiers in microbiology · 2017Article
- Comparative Genomics Identifies a Novel Conserved Protein, HpaT, in Proteobacterial Type III Secretion Systems that Do Not Possess the Putative Translocon Protein HrpF.Frontiers in microbiology · 2017Article
- Type III-Dependent Translocation of HrpB2 by a Nonpathogenic hpaABC Mutant of the Plant-Pathogenic Bacterium Xanthomonas campestris pv. vesicatoria.Applied and environmental microbiology · 2016Article
- HrcU and HrpP are pathogenicity factors in the fire blight pathogen Erwinia amylovora required for the type III secretion of DspA/E.BMC microbiology · 2016Article
- Type Three Secretion System in Attaching and Effacing Pathogens.Frontiers in cellular and infection microbiology · 2016Review
- Xanthomonas campestris pv. vesicatoria Secretes Proteases and Xylanases via the Xps Type II Secretion System and Outer Membrane Vesicles.Journal of bacteriology · 2015Article
- The post-transcriptional regulator rsmA/csrA activates T3SS by stabilizing the 5' UTR of hrpG, the master regulator of hrp/hrc genes, in Xanthomonas.PLoS pathogens · 2014Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Pathogenicity of many Gram-negative bacteria depends on a type III secretion (T3S) system which translocates bacterial effector proteins into eukaryotic cells. The membrane-spanning secretion apparatus is associated with a cytoplasmic ATPase complex and a predicted cytoplasmic (C) ring structure which is proposed to provide a substrate docking platform for secreted proteins. In this study, we show that the putative C ring component HrcQ from the plant pathogenic bacterium Xanthomonas campestris pv. vesicatoria is essential for bacterial pathogenicity and T3S. Fractionation studies revealed that HrcQ localizes to the cytoplasm and associates with the bacterial membranes under T3S-permissive conditions. HrcQ binds to the cytoplasmic T3S-ATPase HrcN, its predicted regulator HrcL and the cytoplasmic domains of the inner membrane proteins HrcV and HrcU. Furthermore, we observed an interaction between HrcQ and secreted proteins including early and late T3S substrates. HrcQ might therefore act as a general substrate acceptor site of the T3S system and is presumably part of a larger protein complex. Interestingly, the N-terminal export signal of the T3S substrate AvrBs3 is dispensable for the interaction with HrcQ, suggesting that binding of AvrBs3 to HrcQ occurs after its initial targeting to the T3S system.
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