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Regulation of expression of the ADE3 gene for yeast C1-tetrahydrofolate synthase, a trifunctional enzyme involved in one-carbon metabolism.
J Biol Chem. 1985 Jan 25; 260(2):1248-56.JB

Abstract

C1-THF (5,6,7,8-tetrahydrofolate) synthase is a trifunctional protein catalyzing the sequential reactions specified by the enzymes 10-formyl-THF synthetase (EC 6.3.4.3), 5,10-methenyl-THF cyclohydrolase (EC 3.5.4.9), and 5,10-methylene-THF dehydrogenase (EC 1.5.1.5). These three activities supply the activated one-carbon units required for the biosynthesis of purines, thymidylate, the amino acids histidine and methionine, the vitamin pantothenic acid, and the formyl group of mitochondrial fMet-tRNAfMet. Extracts of Saccharomyces cerevisiae whose growth is dependent on the three activities of C1-THF synthase contain 2-3 times the level of enzyme activity of extracts from cells grown under conditions where they are independent of this enzyme. Repression of C1-THF synthase activity requires the simultaneous presence of adenine, histidine, methionine, and pantothenic acid. Starvation of the cells for any one of these nutrients leads to derepression of the enzyme. Drug-induced folate starvation also leads to derepression of enzyme activity. The response to changing nutritional conditions occurs within 1 h and is due to changes in the steady-state concentration of C1-THF synthase enzyme, rather than to activation or deactivation of a pre-existing pool of enzyme. Determination of the amount of C1-THF synthase mRNA under the various growth conditions by an in vitro translation/immunoprecipitation assay indicates that regulation of the enzyme occurs predominantly at a pretranslational level since steady-state levels of C1-THF synthase mRNA are 2-3-fold higher in derepressed cells than in repressed cells.

Authors

No affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.

Language

eng

PubMed ID

3881424

Citation

Appling, D R., and J C. Rabinowitz. "Regulation of Expression of the ADE3 Gene for Yeast C1-tetrahydrofolate Synthase, a Trifunctional Enzyme Involved in One-carbon Metabolism." The Journal of Biological Chemistry, vol. 260, no. 2, 1985, pp. 1248-56.
Appling DR, Rabinowitz JC. Regulation of expression of the ADE3 gene for yeast C1-tetrahydrofolate synthase, a trifunctional enzyme involved in one-carbon metabolism. J Biol Chem. 1985;260(2):1248-56.
Appling, D. R., & Rabinowitz, J. C. (1985). Regulation of expression of the ADE3 gene for yeast C1-tetrahydrofolate synthase, a trifunctional enzyme involved in one-carbon metabolism. The Journal of Biological Chemistry, 260(2), 1248-56.
Appling DR, Rabinowitz JC. Regulation of Expression of the ADE3 Gene for Yeast C1-tetrahydrofolate Synthase, a Trifunctional Enzyme Involved in One-carbon Metabolism. J Biol Chem. 1985 Jan 25;260(2):1248-56. PubMed PMID: 3881424.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Regulation of expression of the ADE3 gene for yeast C1-tetrahydrofolate synthase, a trifunctional enzyme involved in one-carbon metabolism. AU - Appling,D R, AU - Rabinowitz,J C, PY - 1985/1/25/pubmed PY - 1985/1/25/medline PY - 1985/1/25/entrez SP - 1248 EP - 56 JF - The Journal of biological chemistry JO - J. Biol. Chem. VL - 260 IS - 2 N2 - C1-THF (5,6,7,8-tetrahydrofolate) synthase is a trifunctional protein catalyzing the sequential reactions specified by the enzymes 10-formyl-THF synthetase (EC 6.3.4.3), 5,10-methenyl-THF cyclohydrolase (EC 3.5.4.9), and 5,10-methylene-THF dehydrogenase (EC 1.5.1.5). These three activities supply the activated one-carbon units required for the biosynthesis of purines, thymidylate, the amino acids histidine and methionine, the vitamin pantothenic acid, and the formyl group of mitochondrial fMet-tRNAfMet. Extracts of Saccharomyces cerevisiae whose growth is dependent on the three activities of C1-THF synthase contain 2-3 times the level of enzyme activity of extracts from cells grown under conditions where they are independent of this enzyme. Repression of C1-THF synthase activity requires the simultaneous presence of adenine, histidine, methionine, and pantothenic acid. Starvation of the cells for any one of these nutrients leads to derepression of the enzyme. Drug-induced folate starvation also leads to derepression of enzyme activity. The response to changing nutritional conditions occurs within 1 h and is due to changes in the steady-state concentration of C1-THF synthase enzyme, rather than to activation or deactivation of a pre-existing pool of enzyme. Determination of the amount of C1-THF synthase mRNA under the various growth conditions by an in vitro translation/immunoprecipitation assay indicates that regulation of the enzyme occurs predominantly at a pretranslational level since steady-state levels of C1-THF synthase mRNA are 2-3-fold higher in derepressed cells than in repressed cells. SN - 0021-9258 UR - https://www.unboundmedicine.com/medline/citation/3881424/Regulation_of_expression_of_the_ADE3_gene_for_yeast_C1_tetrahydrofolate_synthase_a_trifunctional_enzyme_involved_in_one_carbon_metabolism_ L2 - http://www.jbc.org/cgi/pmidlookup?view=long&pmid=3881424 DB - PRIME DP - Unbound Medicine ER -