Disease relevance of folC

• The cloned gene complemented E. coli folC mutations and was found to encode both folylpolyglutamate synthetase and dihydrofolate synthetase activities [1].
• An essential function for Streptomyces folC was suggested by the fact that it could not be mutated using a conventional gene disruption technique [2].
• The deduced folC gene product is a protein of 46,677 Da whose sequence is similar to other folylpolyglutamate synthetases and folylpolyglutamate synthetase-dihydrofolate synthetases from both Gram-positive and Gram-negative bacteria [2].
• Cloning and characterization of the Neisseria gonorrhoeae MS11 folC gene [3].
• An E. coli folC mutant suppressed the phage mutant under conditions where it presumably accumulated methyl-tetrahydrofolate (methyl-THF) [4].

High impact information on folC

• The folC gene from mutant strain SF4 was cloned into a pUC19 plasmid [5].
• Mutant genes with arginine, glutamate, and leucine substitutions, which did not complement the SF4 strain, could complement a folC deletion strain, but produced smaller colonies on complex plates and did not grow on minimal medium [5].
• The folC gene is located about 1 kilobase upstream of the purF gene region at 50 min on the Escherichia coli map [6].
• The folC gene is adjacent to a gene located 70 base pairs upstream of the initiation codon for folC [6].
• The nucleotide sequence of the gene for folylpoly-gamma-glutamate synthetase-dihydrofolate synthetase (folC) has been determined [6].

Chemical compound and disease context of folC

• The Escherichia coli gene for folylpolyglutamate synthetase-dihydrofolate synthetase was localized to plasmids pLC22-45, 24-31, and 28-44 of the Clarke-Carbon E. coli colony bank (Clarke, L., and Carbon, J. (1976) Cell 9, 91-99) by screening the bank by replica mating with an E. coli folC mutant [7].
• Mutant proteins E143A, and even E143D and E143Q with conservative mutations, lacked enzyme activity and failed to complement the methionine auxotrophy of the E. coli folC mutant SF4, showing that Glu143 is an essential residue [8].

Biological context of folC

• Deletion of the upstream gene sequences from recombinant plasmids containing the folC gene results in about a 100-fold decrease in plasmid-dependent folylpolyglutamate synthetase activity, suggesting that the major promoter for folC is 5' to the upstream gene [6].
• Mutagenesis of the folC gene encoding folylpolyglutamate synthetase-dihydrofolate synthetase in Escherichia coli [9].
• The ribosomal binding site of tpc is immediately downstream of the translational stop codon of the folC gene coding for an enzyme involved in folic acid biosynthesis and one-carbon metabolism [10].
• The folylpolyglutamate synthetase-dihydrofolate synthetase gene (folC) in Escherichia coli was deleted from the bacterial chromosome and replaced by a selectable Kmr marker [11].
• It is shown that a third gene, which may overlap the coding sequence of the folC gene by 8 base pairs at the 3' end, nevertheless, has an promoter independent from that of the upstream gene-folC operon [12].

Associations of folC with chemical compounds

• Expression of the upstream gene in maxicells was greater than that of folC, as determined by the intensity of 35S-labeled proteins after sodium dodecyl sulfate-gel electrophoresis [6].

Other interactions of folC

• Analysis of a Streptomyces coelicolor A3(2) locus containing the nucleoside diphosphate kinase (ndk) and folylpolyglutamate synthetase (folC) genes [2].

References