A second Escherichia coli protein with CL synthase activity

Biochim Biophys Acta. 2000 Jan 17;1483(2):263-74. doi: 10.1016/s1388-1981(99)00193-6.

Abstract

The Escherichia coli open reading frame f413, which has the potential to code for a polypeptide homologous to cardiolipin (CL) synthase, has been cloned. Its polypeptide product has a molecular mass of 48 kDa, is membrane-bound, and catalyzes CL formation but does not hydrolyze CL. A comparison of the sequences predicted for the polypeptides encoded by f413 and cls indicates that the N-terminal residues specified by cls may be unnecessary for CL synthase activity. Construction of a truncated cls gene and characterization of its polypeptide product have confirmed this conclusion.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cardiolipins / metabolism
  • Cloning, Molecular
  • Escherichia coli / enzymology
  • Escherichia coli / genetics*
  • Gene Expression
  • Genes, Bacterial
  • Kinetics
  • Membrane Proteins*
  • Mutation
  • Phospholipase D / metabolism
  • Plasmids
  • Temperature
  • Transferases (Other Substituted Phosphate Groups) / chemistry
  • Transferases (Other Substituted Phosphate Groups) / genetics*
  • Transferases (Other Substituted Phosphate Groups) / metabolism

Substances

  • Cardiolipins
  • Membrane Proteins
  • Transferases (Other Substituted Phosphate Groups)
  • cardiolipin synthetase
  • Phospholipase D