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Gene Review

ECs4560  -  protein CesT

Escherichia coli O157:H7 str. Sakai

 
 
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Disease relevance of ECs4560

  • The crystal structures of the enterohemorrhagic Escherichia coli O157:H7 Tir-specific chaperone CesT and the Salmonella enterica SigD-specific chaperone SigE reveal a common overall fold and formation of homodimers [1].
  • Backbone resonance assignment of the homodimeric, 35 kDa chaperone CesT from enteropathogenic Escherichia coli [2].
 

High impact information on ECs4560

  • CesT was also shown to be required for the efficient secretion of several type III effectors encoded within and outside the locus of enterocyte effacement (LEE) in addition to Tir and Map [3].
  • A Tir-CyaA fusion containing the CesT binding domain was translocated into HeLa cells more rapidly in the presence of CesT compared with translocation in the absence of CesT [4].
  • The CesT N-terminal is implicated in chaperone dimerization, whereas the amphipathic alpha-helical region of the C-terminal, is intimately involved in substrate binding [5].
  • Collectively, these results suggest that an N-terminal domain of 26 amino acids functions as a CesT-independent signal that is capable of delivering Tir into both the culture supernatant and the cytosol of host cells [4].
 

Analytical, diagnostic and therapeutic context of ECs4560

  • Isothermal titration calorimetry studies of Tir-CesT and enzymatic activity profiles of SigD-SigE indicate that the effector proteins are not globally unfolded in the presence of their cognate chaperones [1].
  • We showed by affinity chromatography that EscN and Tir bind CesT specifically [6].

References

  1. Structural and biochemical characterization of the type III secretion chaperones CesT and SigE. Luo, Y., Bertero, M.G., Frey, E.A., Pfuetzner, R.A., Wenk, M.R., Creagh, L., Marcus, S.L., Lim, D., Sicheri, F., Kay, C., Haynes, C., Finlay, B.B., Strynadka, N.C. Nat. Struct. Biol. (2001) [Pubmed]
  2. Backbone resonance assignment of the homodimeric, 35 kDa chaperone CesT from enteropathogenic Escherichia coli. Rumpel, S., Kim, H.Y., Vijayan, V., Becker, S., Zweckstetter, M. J. Biomol. NMR (2005) [Pubmed]
  3. CesT is a multi-effector chaperone and recruitment factor required for the efficient type III secretion of both LEE- and non-LEE-encoded effectors of enteropathogenic Escherichia coli. Thomas, N.A., Deng, W., Puente, J.L., Frey, E.A., Yip, C.K., Strynadka, N.C., Finlay, B.B. Mol. Microbiol. (2005) [Pubmed]
  4. The N-terminus of enteropathogenic Escherichia coli (EPEC) Tir mediates transport across bacterial and eukaryotic cell membranes. Crawford, J.A., Kaper, J.B. Mol. Microbiol. (2002) [Pubmed]
  5. Functional analysis of the enteropathogenic Escherichia coli type III secretion system chaperone CesT identifies domains that mediate substrate interactions. Delahay, R.M., Shaw, R.K., Elliott, S.J., Kaper, J.B., Knutton, S., Frankel, G. Mol. Microbiol. (2002) [Pubmed]
  6. Translocated intimin receptor and its chaperone interact with ATPase of the type III secretion apparatus of enteropathogenic Escherichia coli. Gauthier, A., Finlay, B.B. J. Bacteriol. (2003) [Pubmed]
 
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