SwePub - sökning: onr:"swepub:oai:DiVA.org:umu-9...

Numrering	Referens	Omslagsbild	Hitta
1.	Lloyd, Scott A, et al. (författare) Molecular characterization of type III secretion signals via analysis of synthetic N-terminal amino acid sequences 2002 Ingår i: Molecular Microbiology. - : Wiley. - 0950-382X .- 1365-2958. ; 43:1, s. 51-9 Tidskriftsartikel (refereegranskat)abstract 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.

Lloyd, Scott A, et al. (författare)
Molecular characterization of type III secretion signals via analysis of synthetic N-terminal amino acid sequences
2002
Ingår i: Molecular Microbiology. - : Wiley. - 0950-382X .- 1365-2958. ; 43:1, s. 51-9
Tidskriftsartikel (refereegranskat)abstract
- 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.

Träfflista för sökning "onr:"swepub:oai:DiVA.org:umu-9150" "