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 Citations (Scopus)

Abstract

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
JournalBiokhimiya
Volume61
Issue number1
StatePublished - Jan 1996

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Phosphatidylglycerols
Mutant Proteins
Escherichia coli
Alkaline Phosphatase
Phospholipids
Substitution reactions
Amino Acids
Processing
Membranes
Chemical analysis
Arbutin
Cardiolipins
Protein Sorting Signals
Oligosaccharides
Substrates
Enzymes

ASJC Scopus subject areas

  • Chemistry(all)

Cite this

Block of alkaline phosphatase processing due to single amino acid substitutions affects phospholipid composition and turnover in Escherichia coli cells secreting mutant proteins. / Kalinin, A. E.; Karamyshev, A. L.; Nesmeyanova, M. A.

In: Biokhimiya, Vol. 61, No. 1, 01.1996, p. 100-109.

Research output: Contribution to journalArticle

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