Molecular cloning of murine folylpoly-gamma-glutamate synthetase

Biochim Biophys Acta. 1996 Feb 7;1305(1-2):11-4. doi: 10.1016/0167-4781(95)00193-x.

Abstract

Folylpoly-gamma-glutamate synthetase (FPGS) is essential for mammallian cell survival and is a major determinant of cytotoxicity and selectivity for folate antimetabolites. Here we describe the cloning of a cDNA encoding murine FPGS isolated from L1210 leukemia cells. The amino acid sequence of murine FPGS is 82% identical to human FPGS+[1] with identical discrete regions of up to 41 residues. Murine FPGS contains two AUG initiation codons, shown to be responsible for mitochondrial and cytosolic forms of the enzyme in human cells [2] Previous studies indicated species, tissue, and tumor specific differences in mammalian FPGS. The availability of murine FPGS expands the knowledge and understanding of the spectrum of these variations.

Publication types

  • Comparative Study
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Cloning, Molecular
  • DNA, Complementary
  • Escherichia coli / genetics
  • Humans
  • Lactobacillus / enzymology
  • Lactobacillus / genetics
  • Leukemia L1210 / enzymology
  • Leukemia L1210 / genetics
  • Mice
  • Molecular Sequence Data
  • Peptide Synthases / genetics*
  • Sequence Homology, Amino Acid
  • Species Specificity

Substances

  • DNA, Complementary
  • Peptide Synthases
  • folylpolyglutamate synthetase

Associated data

  • GENBANK/U32197