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

Mark Pallen, MS Francis, Klaus Futterer

Research output: Contribution to journalArticle

54 Citations (Scopus)


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.
Original languageEnglish
Pages (from-to)53-60
Number of pages8
JournalFEMS Microbiology Letters
Issue number1
Publication statusPublished - 6 Jun 2003


  • homology modelling
  • protein-protein interaction
  • tetratricopeptide repeat
  • homology search
  • type-III secretion
  • chaperone
  • LcrH


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