Block of alkaline phosphatase processing due to single amino acid substitutions affects phospholipid composition and turnover in Escherichia coli cells secreting mutant proteins

A. E. Kalinin, A. L. Karamyshev, M. A. Nesmeyanova

Research output: Contribution to journalArticle

2 Scopus citations


Amino acid substitutions in the cleavage site of the E. coli alkaline phosphatase signal peptide Val for Ala(-1) or Pro for Arg(+1) result in the block of the enzyme processing. In cells secreting such mutant proteins the relative content and rate of turnover of anionic phospholipids (phosphatidylglycerol and cardiolipin) are increased. The rise of the transfer of the phosphoglycerol residue from phosphatidylglycerol to periplasmic membrane derived oligosaccharides or to the model substrate, arbutin performed by the activity of phosphoglycerol transferase I testifies to phosphatidylglycerol accumulation of the outer surface of the cytoplasmic membrane. The results suggest of phosphatidylglycerol interaction with the alkaline phosphatase precursor and their subsequent joint translocation through the cytoplasmic membrane of E. coli.

Original languageEnglish (US)
Pages (from-to)100-109
Number of pages10
Issue number1
Publication statusPublished - Jan 1996


ASJC Scopus subject areas

  • Chemistry(all)

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