Yersinia enterocolitica type III secretion chaperone SycD: Recombinant expression, purification and characterization of a homodimer

Schmid, Annika; Dittmann, Svea; Grimminger, Valerie; Walter, Stefan; Heesemann, Jürgen; Wilharm, Gottfried

doi:10.1016/j.pep.2006.04.012

Cited by 17 publications

(13 citation statements)

References 37 publications

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“…The truncated SycD structure corroborates the presence of tandem TPRs (17). However, although SycD has been shown to dimerize in solution (19), the structural arrangement in the crystal reveals 3 possible dimers (18). Moreover, how the substrates associate with the class II chaperone is unclear.…”

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confidence: 71%

IpaB–IpgC interaction defines binding motif for type III secretion translocator

Lunelli

Lokareddy

Zychlinsky

et al. 2009

Proc. Natl. Acad. Sci. U.S.A.

191

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The delivery of virulence factors into host cells through type III secretion systems is essential for enterobacterial pathogenesis. Molecular chaperones bind specifically to virulence factors in the bacterial cytosol before secretion. Invasion plasmid gene C (IpgC) is a chaperone that binds 2 essential virulence factors of Shigella: invasion plasmid antigens (Ipa) B and C. Here, we report the crystal structure of IpgC alone and in complex with the chaperone binding domain (CBD) of IpaB. The chaperone captures the CBD in an extended conformation that is stabilized by conserved residues lining the cleft. Analysis of the cocrystal structure reveals a sequence motif that is functional in the IpaB translocator class from different bacteria as determined by isothermal titration calorimetry. Our results show how translocators are chaperoned and may allow the design of inhibitors of enterobacterial diseases.asymmetric homodimer ͉ chaperone ͉ microbiology ͉ pathogens ͉ tetratricopeptide repeat

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mentioning

confidence: 71%

IpaB–IpgC interaction defines binding motif for type III secretion translocator

Lunelli

Lokareddy

Zychlinsky

et al. 2009

Proc. Natl. Acad. Sci. U.S.A.

191

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“…Furthermore, it is not yet known whether this binding is influenced by the presence of LcrQ. This is a critical point considering that SycD (synonymous with LRH) can interact directly with YscM2, one of two LcrQ homologues produced by Yersinia enterocolitica (71,72). We therefore propose to utilize infuture studies, the YopD vari-ants isolated from this present study, which are solely exhibiting yop regulatory defects of varying severity, to better define the contributions of YopD (and LcrH) to post-transcriptional silencing of Yop synthesis.…”

Section: Discussionmentioning

confidence: 99%

YopD Self-assembly and Binding to LcrV Facilitate Type III Secretion Activity by Yersinia pseudotuberculosis

Costa

Edqvist

Bröms

et al. 2010

Journal of Biological Chemistry

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YopD-like translocator proteins encoded by several Gramnegative bacteria are important for type III secretion-dependent delivery of anti-host effectors into eukaryotic cells. This probably depends on their ability to form pores in the infected cell plasma membrane, through which effectors may gain access to the cell interior. In addition, Yersinia YopD is a negative regulator essential for the control of effector synthesis and secretion. As a prerequisite for this functional duality, YopD may need to establish molecular interactions with other key T3S components. A putative coiled-coil domain and an ␣-helical amphipathic domain, both situated in the YopD C terminus, may represent key protein-protein interaction domains. Therefore, residues within the YopD C terminus were systematically mutagenized. All 68 mutant bacteria were first screened in a variety of assays designed to identify individual residues essential for YopD function, possibly by providing the interaction interface for the docking of other T3S proteins. Mirroring the effect of a full-length yopD gene deletion, five mutant bacteria were defective for both yop regulatory control and effector delivery. Interestingly, all mutations clustered to hydrophobic amino acids of the amphipathic domain. Also situated within this domain, two additional mutants rendered YopD primarily defective in the control of Yop synthesis and secretion. Significantly, protein-protein interaction studies revealed that functionally compromised YopD variants were also defective in self-oligomerization and in the ability to engage another translocator protein, LcrV. Thus, the YopD amphipathic domain facilitates the formation of YopD/YopD and YopD/LcrV interactions, two critical events in the type III secretion process.

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“…Interestingly, these chaperones interact with the negative regulators of Yop expression, YscM1 (orthologous to LcrQ of Y. pestis and Y. pseudotuberculosis ) and YscM2, respectively [25,30,31]. YscM2 is only present in Y. enterocolitica and paralogous to YscM1, sharing 57% identical residues [32].…”

Section: Resultsmentioning

confidence: 99%

The Yersinia enterocolitica type three secretion chaperone SycO is integrated into the Yop regulatory network and binds to the Yop secretion protein YscM1

et al. 2007

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Background: Pathogenic yersiniae (Y. pestis, Y. pseudotuberculosis, Y. enterocolitica) share a virulence plasmid encoding a type three secretion system (T3SS). This T3SS comprises more than 40 constituents. Among these are the transport substrates called Yops (Yersinia outer proteins), the specific Yop chaperones (Sycs), and the Ysc (Yop secretion) proteins which form the transport machinery. The effectors YopO and YopP are encoded on an operon together with SycO, the chaperone of YopO. The characterization of SycO is the focus of this study.

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Yersinia enterocolitica type III secretion chaperone SycD: Recombinant expression, purification and characterization of a homodimer

Cited by 17 publications

References 37 publications

IpaB–IpgC interaction defines binding motif for type III secretion translocator

IpaB–IpgC interaction defines binding motif for type III secretion translocator

YopD Self-assembly and Binding to LcrV Facilitate Type III Secretion Activity by Yersinia pseudotuberculosis

The Yersinia enterocolitica type three secretion chaperone SycO is integrated into the Yop regulatory network and binds to the Yop secretion protein YscM1

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