Yersinia enterocolitica type III secretion chaperone SycH. Recombinant expression, purification, characterisation, and crystallisation

Wibke, Neumayer; Groll, M.; Lehmann, Verena; Antoneka, Uladzimir; Kähler, Susanne; Heesemann, Jürgen; Wilharm, Gottfried

doi:10.1016/j.pep.2004.02.017

Cited by 6 publications

(10 citation statements)

References 37 publications

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“…This suggests that it is the chaperone that directs the effector toward the ATPase. This finding is in line with our recently presented model of type III secretion, predicting that TTSS ATPases act as unfoldases using the TTSS chaperones to encounter the secretion substrates (21,24,43). After displacement of the chaperone by the ATPase, the chaperone-binding site of the effector, lacking tertiary structure, is distinguished as an ideal starting point for unraveling the effector.…”

Section: Discussionsupporting

confidence: 87%

“…A on the conformation of their substrates is restricted to the binding sites identified close to the N termini (9,14,17,21,24). Here, for the first time, an interaction between the catalytic domain of an effector, YopT, and its specific chaperone, SycT, was revealed.…”

Section: Discussionmentioning

confidence: 91%

“…ComplexesWork from several groups suggests that the influence of class I TTSS chaperones on the folding of their substrates is restricted to the binding site generally encompassing about 50 -100 amino acid residues (9,14,17,21,24). To understand the functioning of these chaperones, high resolution structural data on complete type III effectors in complex with their respective chaperones are required.…”

Section: Co-expression and Purification Of Yopt/syctmentioning

confidence: 99%

“…The SycN/YscB complex is an exception in that SycN and YscB form a heterodimer (17) with a fold similar to that of the typical homodimers. The SycH fold also resembles that of the aforementioned chaperones (16); however, its biologically relevant oligomerization state is not unambiguously clear (21). The fold of the class IB chaperone Spa15 is very similar to that of class IA chaperones; dimer formation, however, is different, with the subunits rotated relative to each other (19).…”

mentioning

confidence: 99%

“…The effector domain is wrapped around the chaperone dimer in an expanded form retaining secondary structure elements. Work from several groups further suggests that the C-terminally located effector domains are folded and catalytically active in the presence of their respective chaperones (9,14,21,24). Only recently, the structure of the secretable regulatory TTSS component YopN from Yersinia in complex with the heterodimeric chaperone SycN/YscB was presented (17).…”

mentioning

confidence: 99%

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Crystal Structure of the Yersinia enterocolitica Type III Secretion Chaperone SycT

Locher

Lehnert

Krauss

et al. 2005

Journal of Biological Chemistry

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Several Gram-negative pathogens deploy type III secretion systems (TTSSs) as molecular syringes to inject effector proteins into host cells. Prior to secretion, some of these effectors are accompanied by specific type III secretion chaperones. The Yersinia enterocolitica TTSS chaperone SycT escorts the effector YopT, a cysteine protease that inactivates the small GTPase RhoA of targeted host cells. We solved the crystal structure of SycT at 2.5 Å resolution. Despite limited sequence similarity among TTSS chaperones, the SycT structure revealed a global fold similar to that exhibited by other structurally solved TTSS chaperones. The dimerization domain of SycT, however, differed from that of all other known TTSS chaperone structures. Thus, the dimerization domain of TTSS chaperones does not likely serve as a general recognition pattern for downstream processing of effector/chaperone complexes. Yersinia Yop effectors are bound to their specific Syc chaperones close to the Yop N termini, distinct from their catalytic domains. Here, we showed that the catalytically inactive YopT C139S is reduced in its ability to bind SycT, suggesting an ancillary interaction between YopT and SycT. This interaction could maintain the protease inactive prior to secretion or could influence the secretion competence and folding of YopT.

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Section: Discussionsupporting

confidence: 87%