Amino-terminal sequence analysis of four plasmid-encoded virulence-associated proteins of Salmonella typhimurium.
We have expressed four virulence-associated proteins encoded by the Salmonella typhimurium plasmid pEX102 in Escherichia coli. The genes coding for the proteins MkaA, MkaB, MkaC and MkaD subcloned in the vectors pUC19 or Bluescript KS+ directed substantial production of these proteins in E. coli. The same host harbouring pEX102 did not produce these proteins in detectable amounts. The proteins were exclusively found in the particulate fraction. The amino-terminal sequence analysis showed that the N-termini of these proteins corresponded to the ones predicted from the open reading frames found previously in the DNA sequence of the virulence determinant and that no N-terminal signal sequence processing of the proteins occurred.
Taira
S
S
National Public Health Institute, Molecular Biology Unit, Helsinki, Finland.
Baumann
M
M
Riikonen
P
P
Sukupolvi
S
S
Rhen
M
M
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000235:genetics*; D003001:Cloning, Molecular; D004926:Escherichia coli / Q000235:genetics; D008969:Molecular Sequence Data; D010957:Plasmids; D012486:Salmonella typhimurium / Q000235:genetics* / Q000472:pathogenicity; D014157:Transcription Factors; D014774:Virulence / Q000235:genetics
D001426:Bacterial Proteins; D014157:Transcription Factors; C061929:mkaB protein, Salmonella typhimurium; C061928:mkaC protein, Salmonella typhimurium; C068962:MkaA protein, Salmonella typhimurium; C068963:MkaD protein, Salmonella typhimurium