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Molecular characterization of type III secretion signals via analysis of synthetic N-terminal amino acid sequences
Umeå University, Faculty of Science and Technology, Department of Molecular Biology (Faculty of Science and Technology).
Umeå University, Faculty of Science and Technology, Department of Chemistry.
Umeå University, Faculty of Science and Technology, Department of Molecular Biology (Faculty of Science and Technology).
Umeå University, Faculty of Science and Technology, Department of Molecular Biology (Faculty of Science and Technology).
2002 (English)In: Molecular Microbiology, Vol. 43, no 1, 51-9 p.Article in journal (Refereed) Published
Abstract [en]

Yersinia species utilize a type III secretion system to inject toxins, called Yops (Yersinia outer proteins), into eukaryotic cells. The N-termini of the Yops serve as type III secretion signals, but they do not share a consensus sequence. To simplify the analysis of type III secretion signals, we replaced amino acids 2–8 of the secreted protein YopE with all permutations (27 or 128) of synthetic serine/isoleucine sequences. The results demonstrate that amphipathic N-terminal sequences, containing four or five serine residues, have a much greater probability than hydrophobic or hydrophilic sequences to target YopE for secretion. Multiple linear regression analysis of the synthetic sequences was used to obtain a model for N-terminal secretion signals. The model accurately classifies the N-terminal sequences of native type III substrates as efficient secretion signals.

Place, publisher, year, edition, pages
2002. Vol. 43, no 1, 51-9 p.
Identifiers
URN: urn:nbn:se:umu:diva-9150DOI: 10.1046/j.1365-2958.2002.02738.xOAI: oai:DiVA.org:umu-9150DiVA: diva2:148821
Available from: 2008-03-04 Created: 2008-03-04 Last updated: 2013-03-19Bibliographically approved

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Sjöström, MichaelWolf-Watz, Hans
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