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Volume 142, Issue 4

Surface location of HPr, a phosphocarrier of the phosphoenolpyruvate: sugar phosphotransferase system in Free

Abstract

HPr is a low-molecular-mass phosphocarrier protein of the bacterial phosphoenolpyruvate (PEP): sugar phosphotransferase system (PTS) found in the cytoplasm or associated with the inner surface of the cytoplasmic membrane. Treatment of cells with a Sorvall Omnimixer, a technique used to extract cell surface components, resulted in the extraction of a major protein with a molecular mass of 9 kDa. Several lines of evidence suggested that this protein was HPr: (i) the protein showed homology over the first 35 N-terminal amino acid residues with the HPrs of and , including the signature sequence for the site of PEP-dependent phosphorylation; (ii) it cross-reacted with the anti-HPr antibody preparation; (iii) it could be phosphorylated by enzyme 1 at the expense of PEP, and by a membrane-associated kinase at the expense of ATP; and (iv) it possessed phosphocarrier activity when used as a source of HPr in an PTS assay. The data suggested that a portion of the cellular HPr is associated with the external cell surface in , a result that was confirmed by immunogold electron microscopy. The cellular HPr of consisted of two forms that could be distinguished by the presence or the absence of the N-terminal methionine. Amino acid sequence analysis indicated that the cell-surface-associated HPr of lacked the N-terminal methionine residue.

  • Received:
  • Accepted:
  • Revised:
  • Published Online:
Keyword(s): cell surface proteins , HPr , methionine aminopeptidase , phospotransferase system and Streptococcus suis.
© Society for General Microbiology 1996
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1996-04-01
2024-04-24
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Surface location of HPr, a phosphocarrier of the phosphoenolpyruvate: sugar phosphotransferase system in Streptococcus suis
Microbiology 142, 837 (1996); https://doi.org/10.1099/00221287-142-4-837
/content/journal/micro/10.1099/00221287-142-4-837
/content/journal/micro/10.1099/00221287-142-4-837
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