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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 

Identification of methionine-processed HPr in the equine pathogen Streptococcus equi.

Using preparative electrophoresis, a low molecular weight protein has been partially purified from a cell extract of the equine pathogen Streptococcus equi susp. equi. N-terminal sequence analysis and Western blotting revealed the protein to be HPr, a central component of the phosphoenolpyruvate:sugar phosphotransferase system (PTS). Interestingly, the only form of the HPr protein detected in S. equi was one with the amino-terminal methionine removed, a modification that has previously been associated with surface localization of streptococcal HPr proteins.[1]

References

  1. Identification of methionine-processed HPr in the equine pathogen Streptococcus equi. Sutcliffe, I.C., Trigg, J., Harrington, D. Syst. Appl. Microbiol. (2000) [Pubmed]
 
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