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- W2127788339 abstract "Summary The plant pathogenic bacterium Xanthomonas campestris pv. vesicatoria utilizes a type III secretion (T3S) system to inject effector proteins into eukaryotic cells. T3S substrate specificity is controlled by HpaC, which promotes secretion of translocon and effector proteins but prevents efficient secretion of the early substrate HrpB2. HpaC and HrpB2 interact with the C‐terminal domain (HrcU C ) of the FlhB/YscU homologue HrcU. Here, we provide experimental evidence that HrcU is proteolytically cleaved at the conserved NPTH motif, which is required for binding of both HpaC and HrpB2 to HrcU C . The results of mutant studies showed that cleavage of HrcU contributes to pathogenicity and secretion of late substrates but is dispensable for secretion of HrpB2, which is presumably secreted prior to HrcU cleavage. The introduction of a point mutation (Y318D) into HrcU C activated secretion of late substrates in the absence of HpaC and suppressed the hpaC mutant phenotype. However, secretion of HrpB2 was unaffected by HrcU Y318D , suggesting that the export of early and late substrates is controlled by independent mechanisms that can be uncoupled. As HrcU Y318D did not interact with HrpB2 and HpaC, we propose that the substrate specificity switch leads to the release of HrcU C ‐bound HrpB2 and HpaC." @default.
- W2127788339 created "2016-06-24" @default.
- W2127788339 creator A5050164204 @default.
- W2127788339 creator A5055624829 @default.
- W2127788339 date "2010-11-24" @default.
- W2127788339 modified "2023-10-16" @default.
- W2127788339 title "Secretion of early and late substrates of the type III secretion system from Xanthomonas is controlled by HpaC and the C-terminal domain of HrcU" @default.
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- W2127788339 doi "https://doi.org/10.1111/j.1365-2958.2010.07461.x" @default.
- W2127788339 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3040844" @default.
- W2127788339 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/21219463" @default.
- W2127788339 hasPublicationYear "2010" @default.
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