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Tetratricopeptide-like repeats in type-III-secretion chaperones and regulators
Umeå University, Faculty of Science and Technology, Department of Molecular Biology (Faculty of Science and Technology).
2003 (English)In: FEMS Microbiology Letters, ISSN 0378-1097, E-ISSN 1574-6968, Vol. 223, no 1, 53-60 p.Article in journal (Refereed) Published
Abstract [en]

Efficient type-III secretion depends on cytosolic molecular chaperones, which bind specifically to the translocators and effectors. In the past there has been a tendency to shoe-horn all type-III-secretion chaperones into a single structural and functional class. However, we have shown that the LcrH/SycD-like chaperones consist of three central tetratricopeptide-like repeats that are predicted to fold into an all-alpha-helical array that is quite distinct from the known structure of the SycE class of chaperones. Furthermore, we predict that this array creates a peptide-binding groove that is utterly different from the helix-binding groove in SycE. We present a homology model of LcrH/SycD that is consistent with existing mutagenesis data. We also report the existence of tetratricopeptide-like repeats in regulators of type-III secretion, such as HilA from Salmonella enterica and HrpB from Ralstonia solanacearum. The discovery of tetratricopeptide-like repeats in type-III-secretion regulators and chaperones provides a new conceptual framework for structural and mutagenesis studies and signals a potential unification of prokaryotic and eukaryotic chaperone biology.

Place, publisher, year, edition, pages
2003. Vol. 223, no 1, 53-60 p.
Keyword [en]
Tetratricopeptide repeat, Type-III secretion, Chaperone, Homology search, Homology modelling, LcrH, Protein–protein interaction
National Category
Microbiology in the medical area
Research subject
Infectious Diseases
URN: urn:nbn:se:umu:diva-41862DOI: 10.1016/S0378-1097(03)00344-6PubMedID: 12799000OAI: diva2:407969
Available from: 2011-04-18 Created: 2011-04-01 Last updated: 2011-04-18Bibliographically approved

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Francis, Matthew S
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