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Gene Review:

sycE - SycE

Yersinia enterocolitica

Birtalan, S. et al., Cheng, L.W. et al., Birtalan, S.C. et al., Evdokimov, A.G. et al., Lee, V.T. et al., et al.

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Disease relevance of sycE

Here we present biochemical and crystallographic results on the Yersinia SycE-YopE chaperone-effector complex that contradict previous models of chaperone function and demonstrate that chaperone action is isolated to only a small portion of the effector [1].

High impact information on sycE

We present the 1.74 A resolution crystal structure of the Yersinia pseudotuberculosis chaperone SycE, whose action in promoting translocation of YopE into host macrophages is essential to Yersinia pathogenesis [2].
SycE, a compact, globular dimer with a novel fold, has two large hydrophobic surface patches that may form binding sites for YopE or other type III components [2].
Yersinia enterocolitica type III secretion. On the role of SycE in targeting YopE into HeLa cells [3].
As compared with wild-type SycE, glutathione S-transferase-SycE bound and stabilized YopE in the bacterial cytoplasm but failed to release the polypeptide for export by the type III machinery [3].
When bound to SycE chaperone in the Yersinia cytoplasm, YopE residues 1-100 are necessary and sufficient for the targeting of hybrid neomycin phosphotransferase [4].

Biological context of sycE

SycE possesses a novel fold with an unusual dimerization motif and an intriguing basic cavity located on the dyad axis of the dimer that may participate in its interaction with YopE [5].

Anatomical context of sycE

Competition between the Yops of Yersinia enterocolitica for delivery into eukaryotic cells: role of the SycE chaperone binding domain of YopE [6].

References

Three-dimensional secretion signals in chaperone-effector complexes of bacterial pathogens. Birtalan, S.C., Phillips, R.M., Ghosh, P. Mol. Cell (2002) [Pubmed]
Structure of the Yersinia type III secretory system chaperone SycE. Birtalan, S., Ghosh, P. Nat. Struct. Biol. (2001) [Pubmed]
Yersinia enterocolitica type III secretion. On the role of SycE in targeting YopE into HeLa cells. Cheng, L.W., Schneewind, O. J. Biol. Chem. (1999) [Pubmed]
Targeting of Yersinia Yop proteins into the cytosol of HeLa cells: one-step translocation of YopE across bacterial and eukaryotic membranes is dependent on SycE chaperone. Lee, V.T., Anderson, D.M., Schneewind, O. Mol. Microbiol. (1998) [Pubmed]
Three-dimensional structure of the type III secretion chaperone SycE from Yersinia pestis. Evdokimov, A.G., Tropea, J.E., Routzahn, K.M., Waugh, D.S. Acta Crystallogr. D Biol. Crystallogr. (2002) [Pubmed]
Competition between the Yops of Yersinia enterocolitica for delivery into eukaryotic cells: role of the SycE chaperone binding domain of YopE. Boyd, A.P., Lambermont, I., Cornelis, G.R. J. Bacteriol. (2000) [Pubmed]

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