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FEMS Microbiol Lett. 2003 Jun 6;223(1):53-60.

Tetratricopeptide-like repeats in type-III-secretion chaperones and regulators.

Author information

1
Division of Immunity and Infection, Medical School, University of Birmingham, Birmingham, B15 2TT, UK. mpallen@bham.ac.uk

Abstract

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.

PMID:
12799000
DOI:
10.1016/S0378-1097(03)00344-6
[Indexed for MEDLINE]
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