Molecular cloning of murine folylpoly-γ-glutamate synthetase

Folylpoly-γ-glutamate synthetase (FPGS) is essential for mammalian 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 FP...

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Bibliographic Details
Published in:Biochimica et biophysica acta 1996-02, Vol.1305 (1), p.11-14
Main Authors: Spinella, Michael J., Brigle, Kevin E., David Goldman, I.
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Base Sequence
cDNA (murine)
Cloning, Molecular
DNA, Complementary
Escherichia coli - genetics
Folylpolyglutamate synthetase
Humans
L1210
Lactobacillus - enzymology
Lactobacillus - genetics
Leukemia L1210 - enzymology
Leukemia L1210 - genetics
Mice
Molecular Sequence Data
Peptide Synthases - genetics
Sequence Homology, Amino Acid
Species Specificity
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Summary:Folylpoly-γ-glutamate synthetase (FPGS) is essential for mammalian 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.
ISSN:0167-4781
0006-3002
1879-2634
DOI:10.1016/0167-4781(95)00193-X