Molecular characterization of type III secretion signals via analysis of synthetic N-terminal amino acid sequences
2002 (English)In: Molecular Microbiology, Vol. 43, no 1, 51-9 p.Article in journal (Refereed) Published
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.
IdentifiersURN: urn:nbn:se:umu:diva-9150DOI: 10.1046/j.1365-2958.2002.02738.xOAI: oai:DiVA.org:umu-9150DiVA: diva2:148821