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Function of yeast cytoplasmic C1-tetrahydrofolate synthase
1Department of Molecular and Cell Biology, University of California, Berkeley 94720.
Summary
The catalytic activity of yeast C1-tetrahydrofolate (THF) synthase is crucial for purine biosynthesis. Its synthetase or dehydrogenase/cyclohydrolase domains are sufficient to complement adenine deficiency in ade3 strains.
Area of Science:
- Biochemistry
- Molecular Biology
- Yeast Genetics
Background:
- The ADE3 gene in Saccharomyces cerevisiae encodes a trifunctional C1-tetrahydrofolate (THF) synthase.
- Previous research suggested ADE3's role in purine biosynthesis complex integrity, not catalytic activity.
Purpose of the Study:
- To investigate the role of yeast C1-tetrahydrofolate (THF) synthase catalytic activity in purine biosynthesis.
- To determine if specific domains of C1-THF synthase are sufficient for complementing adenine auxotrophy.
Main Methods:
- Deletion analysis of the ADE3 gene in yeast.
- Heterologous expression of monofunctional synthetases in ade3 strains.
Main Results:
- Deletion analysis showed either synthetase or dehydrogenase/cyclohydrolase domains complemented the adenine requirement.
- Heterologous expression of monofunctional synthetases indicated high synthetase activity correlated with growth in adenine-deficient media.
Conclusions:
- The catalytic activity of C1-tetrahydrofolate (THF) synthase is essential for purine biosynthesis.
- Both synthetase and dehydrogenase/cyclohydrolase activities contribute to purine synthesis in yeast.