HPr polymorphism in oral streptococci is caused by the partial removal of the N-terminal methionine.
HPr is a small phosphocarrier protein of the bacterial phosphoenolpyruvate:sugar phosphotransferase system involved in the transport and phosphorylation of sugars. It has recently been reported that streptococci possess two forms of HPr having identical biochemical properties. In this communication, we show by N-terminal amino-acid sequencing and by ion-spray mass spectroscopy that these two forms differ by the presence or the absence of the N-terminal methionine.
Vadeboncoeur
C
C
Department of Biochemistry (Sciences) and Dental School, Université Laval, Québec, Canada.
Konishi
Y
Y
Dumas
F
F
Gauthier
L
L
Frenette
M
M
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry*; D013058:Mass Spectrometry / Q000379:methods; D008715:Methionine / Q000737:chemistry*; D008969:Molecular Sequence Data; D010731:Phosphoenolpyruvate Sugar Phosphotransferase System / Q000737:chemistry* / Q000235:genetics; D011110:Polymorphism, Genetic; D013291:Streptococcus / Q000235:genetics*
D001426:Bacterial Proteins; D008715:Methionine; D010731:Phosphoenolpyruvate Sugar Phosphotransferase System; C030182:phosphocarrier protein HPr