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Function of yeast cytoplasmic C1-tetrahydrofolate synthase.
Proc Natl Acad Sci U S A. 1993 Apr 01; 90(7):2636-40.PN

Abstract

The protein product of the ADE3 gene of the yeast Saccharomyces cerevisiae has been identified as the cytoplasmic trifunctional C1-tetrahydrofolate (THF) synthase, which possesses 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) activities. However, it has been suggested that the ADE3-encoded C1-THF synthase does not play a role in providing the enzymes involved in the generation of one-carbon intermediates in the biosynthesis of the purine bases but functions in maintaining the structural integrity of the enzyme complex involved in purine biosynthesis [Barlowe, C. K. & Appling, D. A. (1990) Mol. Cell. Biol. 10, 5679-5687]. This hypothesis is based on their finding that the presence of the full-length ADE3 C1-THF synthase, whether catalytically active or not, is correlated with the Ade+ phenotype. In contrast to their results, our deletion analysis of the ADE3 gene indicates that the presence of either the synthetase or dehydrogenase/cyclohydrolase domains of C1-THF synthase is enough to complement the adenine requirement in ade3 strains. These results are also consistent with those obtained in heterologous expression of spinach and Clostridium acidiurici monofunctional synthetases in ade3 strains. Heterologous expression studies show that the high synthetase activity may be correlated with the increased growth in medium lacking adenine. These results suggest that the catalytic activity of the C1-THF synthase is involved in purine biosynthesis.

Authors+Show Affiliations

Department of Molecular and Cell Biology, University of California, Berkeley 94720.No affiliation info available

Pub Type(s)

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

Language

eng

PubMed ID

8464869

Citation

Song, J M., and J C. Rabinowitz. "Function of Yeast Cytoplasmic C1-tetrahydrofolate Synthase." Proceedings of the National Academy of Sciences of the United States of America, vol. 90, no. 7, 1993, pp. 2636-40.
Song JM, Rabinowitz JC. Function of yeast cytoplasmic C1-tetrahydrofolate synthase. Proc Natl Acad Sci USA. 1993;90(7):2636-40.
Song, J. M., & Rabinowitz, J. C. (1993). Function of yeast cytoplasmic C1-tetrahydrofolate synthase. Proceedings of the National Academy of Sciences of the United States of America, 90(7), 2636-40.
Song JM, Rabinowitz JC. Function of Yeast Cytoplasmic C1-tetrahydrofolate Synthase. Proc Natl Acad Sci USA. 1993 Apr 1;90(7):2636-40. PubMed PMID: 8464869.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Function of yeast cytoplasmic C1-tetrahydrofolate synthase. AU - Song,J M, AU - Rabinowitz,J C, PY - 1993/4/1/pubmed PY - 1993/4/1/medline PY - 1993/4/1/entrez SP - 2636 EP - 40 JF - Proceedings of the National Academy of Sciences of the United States of America JO - Proc. Natl. Acad. Sci. U.S.A. VL - 90 IS - 7 N2 - The protein product of the ADE3 gene of the yeast Saccharomyces cerevisiae has been identified as the cytoplasmic trifunctional C1-tetrahydrofolate (THF) synthase, which possesses 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) activities. However, it has been suggested that the ADE3-encoded C1-THF synthase does not play a role in providing the enzymes involved in the generation of one-carbon intermediates in the biosynthesis of the purine bases but functions in maintaining the structural integrity of the enzyme complex involved in purine biosynthesis [Barlowe, C. K. & Appling, D. A. (1990) Mol. Cell. Biol. 10, 5679-5687]. This hypothesis is based on their finding that the presence of the full-length ADE3 C1-THF synthase, whether catalytically active or not, is correlated with the Ade+ phenotype. In contrast to their results, our deletion analysis of the ADE3 gene indicates that the presence of either the synthetase or dehydrogenase/cyclohydrolase domains of C1-THF synthase is enough to complement the adenine requirement in ade3 strains. These results are also consistent with those obtained in heterologous expression of spinach and Clostridium acidiurici monofunctional synthetases in ade3 strains. Heterologous expression studies show that the high synthetase activity may be correlated with the increased growth in medium lacking adenine. These results suggest that the catalytic activity of the C1-THF synthase is involved in purine biosynthesis. SN - 0027-8424 UR - https://www.unboundmedicine.com/medline/citation/8464869/Function_of_yeast_cytoplasmic_C1_tetrahydrofolate_synthase_ L2 - http://www.pnas.org/cgi/pmidlookup?view=long&pmid=8464869 DB - PRIME DP - Unbound Medicine ER -