Mapping of a YscY Binding Domain within the LcrH Chaperone That Is Required for Regulation of
            <i>Yersinia</i>
            Type III Secretion

Bröms, Jeanette E.; Edqvist, Petra J.; Carlsson, Katrin E.; Forsberg, Åke; Francis, Matthew S.

doi:10.1128/jb.187.22.7738-7752.2005

Cited by 23 publications

(46 citation statements)

References 82 publications

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“…The ␤-galactosidase activity assay indicated that there were strong interactions between PopN and Pcr1, as well as between Pcr3 and Pcr4, consistent with previous reports of Pcr3-Pcr4 interactions, as well as similar interactions in Yersinia (YopN-TyeA and YscX-YscY interactions) (5,25). Most interestingly, we found a novel protein-protein interaction between Pcr1 and Pcr4 linking a chain of interactions, namely PopN-Pcr1-Pcr4-Pcr3.…”

Section: Discussionsupporting

confidence: 78%

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Regulatory Role of PopN and Its Interacting Partners in Type III Secretion of Pseudomonas aeruginosa

et al. 2007

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The type III secretion system (T3SS) of Pseudomonas aeruginosa plays a significant role in pathogenesis. We have previously identified type III secretion factor (TSF), which is required for effective secretion of the type III effector molecules, in addition to the low calcium signal. TSF includes many low-affinity high-capacity calcium binding proteins, such as serum albumin and casein. A search for the TSF binding targets on the bacterial outer membrane resulted in identification of PopN, a component of the T3SS that is readily detectable on the bacterial cell surface. PopN specifically interacts with Pcr1, and both popN and pcr1 mutants have a constitutive type III secretion phenotype, suggesting that the two proteins form a complex that functions as a T3SS repressor. Further analysis of the popN operon genes resulted in identification of protein-protein interactions between Pcr1 and Pcr4 and between Pcr4 and Pcr3, as well as between PopN and Pcr2 in the presence of PscB. Unlike popN and pcr1 mutants, pcr3 and pcr4 mutants are totally defective in type III secretion, while a pcr2 mutant exhibits reduced type III secretion. Interestingly, PopN, Pcr1, Pcr2, and Pcr4 are all secreted in a type III secretion machinery-dependent manner, while Pcr3 is not. These findings imply that these components have important regulatory roles in controlling type III secretion.

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Section: Discussionsupporting

confidence: 78%

“…The observed protein interaction chain may well represent part of a complex controlling type III secretion. Studies have suggested that in Yersinia the LcrH-YscY-YscX and LcrH-YopD-LcrQ regulatory loops are involved in regulating gene expression and the ordered secretion of type III substrates (2,5,6,13).…”

Section: Discussionmentioning

confidence: 99%

Regulatory Role of PopN and Its Interacting Partners in Type III Secretion of Pseudomonas aeruginosa

et al. 2007

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“…Whereas IpgC/SicA function as co-activators for transcription, LcrH functions as the post-transcriptional level to repress yop translation. In contrast, the LcrH homolog from P. aeruginosa (PcrH) lacks detectable regulatory activity [43,44]. This diversity likely reflects environmental pressures that have allowed each pathogen to fine tune gene expression patterns to meet the demands of specific niches.…”

Section: Discussionmentioning

confidence: 99%

Control of gene expression by type III secretory activity

Brutinel

Yahr

2008

Current Opinion in Microbiology

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SummaryThe bacterial flagellum and the highly related injectisome (or needle complex) are among the most complicated multi-protein structures found in Gram-negative microorganisms. The assembly of both structures is dependent upon a type III secretion system. An interesting regulatory feature unique to these systems is the coordination of gene expression with type III secretory activity. This means of regulation ensures that secretion substrates are expressed only when required during the assembly process or upon completion of the fully functional structure. Prominent within the regulatory scheme are secreted proteins and type III secretion chaperones that exert effects on gene expression at the transcriptional and post-transcriptional levels. Although the major structural components of the flagellum and injectisome systems are highly conserved, recent studies reveal diversity in the mechanisms used by secretion substrates and chaperones to control gene expression.

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“…7). Furthermore, LcrH might have an additional regulatory role in the suppression of yop gene expression that is independent of its binding to YopD and involves an interaction of LcrH with YscY, a predicted chaperone of the secreted YscX protein (56,127,181).…”

Section: Control Of Yop Gene Expression In Yersinia Sppmentioning

confidence: 99%

Protein Export According to Schedule: Architecture, Assembly, and Regulation of Type III Secretion Systems from Plant- and Animal-Pathogenic Bacteria

Büttner

2012

Microbiol Mol Biol Rev

359

482

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SUMMARY Flagellar and translocation-associated type III secretion (T3S) systems are present in most Gram-negative plant- and animal-pathogenic bacteria and are often essential for bacterial motility or pathogenicity. The architectures of the complex membrane-spanning secretion apparatuses of both systems are similar, but they are associated with different extracellular appendages, including the flagellar hook and filament or the needle/pilus structures of translocation-associated T3S systems. The needle/pilus is connected to a bacterial translocon that is inserted into the host plasma membrane and mediates the transkingdom transport of bacterial effector proteins into eukaryotic cells. During the last 3 to 5 years, significant progress has been made in the characterization of membrane-associated core components and extracellular structures of T3S systems. Furthermore, transcriptional and posttranscriptional regulators that control T3S gene expression and substrate specificity have been described. Given the architecture of the T3S system, it is assumed that extracellular components of the secretion apparatus are secreted prior to effector proteins, suggesting that there is a hierarchy in T3S. The aim of this review is to summarize our current knowledge of T3S system components and associated control proteins from both plant- and animal-pathogenic bacteria.

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Mapping of a YscY Binding Domain within the LcrH Chaperone That Is Required for Regulation of Yersinia Type III Secretion

Cited by 23 publications

References 82 publications

Regulatory Role of PopN and Its Interacting Partners in Type III Secretion of Pseudomonas aeruginosa

Regulatory Role of PopN and Its Interacting Partners in Type III Secretion of Pseudomonas aeruginosa

Control of gene expression by type III secretory activity

Protein Export According to Schedule: Architecture, Assembly, and Regulation of Type III Secretion Systems from Plant- and Animal-Pathogenic Bacteria

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