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Tetratricopeptide-like repeats in type-III-secretion chaperones and regulators
Umeå universitet, Teknisk-naturvetenskapliga fakulteten, Institutionen för molekylärbiologi (Teknisk-naturvetenskaplig fakultet).
2003 (engelsk)Inngår i: FEMS Microbiology Letters, ISSN 0378-1097, E-ISSN 1574-6968, Vol. 223, nr 1, s. 53-60Artikkel i tidsskrift (Fagfellevurdert) 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.

sted, utgiver, år, opplag, sider
2003. Vol. 223, nr 1, s. 53-60
Emneord [en]
Tetratricopeptide repeat, Type-III secretion, Chaperone, Homology search, Homology modelling, LcrH, Protein–protein interaction
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URN: urn:nbn:se:umu:diva-41862DOI: 10.1016/S0378-1097(03)00344-6PubMedID: 12799000OAI: oai:DiVA.org:umu-41862DiVA, id: diva2:407969
Tilgjengelig fra: 2011-04-18 Laget: 2011-04-01 Sist oppdatert: 2018-06-08bibliografisk kontrollert

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