We intend to test the hypothesis we formulated based on our previous identification of the ribosome binding sites of mRNAs derived from a plasmid gene and two phage genes related to Gram-positive organisms. For this purpose, we will determine the base sequence of binding sites of mRNAs derived from Gram-positive organisms, with particular interest in obtaining examples related to cellular genes of these organisms. The B. subtilis DNA phage 029 will be used as a model system for studying regulation of early and late gene expression in Gram-positive systems. We will attempt to clone the Clostridium acidi-urici ferredoxin gene in order to be able to study the biosynthesis of this model iron-sulfur protein. We will investigate the domain organization of the trifunctional enzyme, C1-synthase, which contains formyltetrahydrofolate synthetase activity as well as methylene-THF dehydrogenase and methenyl-THF cyclohydrolase acitivity. This will be done through the use of a plasmid that has been constructed containing the yeast gene coding for this protein. We will determine whether C1-synthase is associated in any way with other enzymes involved in one-carbon metabolism, and whether the activities of the eucaryotic enzymes are affected by different factors or in different ways from the equivalent single function proteins that occur in procaryotes.
|Song, J M; Cheung, E; Rabinowitz, J C (1996) Organization and characterization of the two yeast ribosomal protein YL19 genes. Curr Genet 30:273-8|
|Song, J M; Cheung, E; Rabinowitz, J C (1995) Nucleotide sequence and characterization of the Saccharomyces cerevisiae RPL19A gene encoding a homolog of the mammalian ribosomal protein L19. Yeast 11:383-9|
|Song, J M; Rabinowitz, J C (1995) The N-terminal, dehydrogenase/cyclohydrolase domain of yeast cytoplasmic trifunctional C1-tetrahydrofolate synthase requires the C-terminal, synthetase domain for the catalytic activity in vitro. FEBS Lett 376:229-32|