Tetratricopeptide-like repeats in type-III-secretion chaperones and regulators
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
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.
Tetratricopeptide repeat, Type-III secretion, Chaperone, Homology search, Homology modelling, LcrH, Protein–protein interaction
Microbiology in the medical area
Research subject Infectious Diseases
IdentifiersURN: urn:nbn:se:umu:diva-41862DOI: 10.1016/S0378-1097(03)00344-6PubMedID: 12799000OAI: oai:DiVA.org:umu-41862DiVA: diva2:407969