| Budget Amount *help |
¥2,100,000 (Direct Cost: ¥2,100,000)
Fiscal Year 1995: ¥700,000 (Direct Cost: ¥700,000)
Fiscal Year 1994: ¥1,400,000 (Direct Cost: ¥1,400,000)
|
|---|
| Research Abstract |
Phosphorylation has been established as a major mechanism by which metabolic processes are regulated. Many factors concerning protein biosynthesis are regulated by phosphorylation and dephosphorylation : aminoacyl-tRNA synthetase, initiation factors, elongation factors EF-1 and EF-2, and ribosomal proteins are regulated by various protein kinases. In the present research the mechanism of translational control by the phosphorylation of elongation factor EF-1 beta has been analyzed.
Casein kinase-like EF-1 beta kinase which phosphorylates beta subunit of EF-1 (EF-1 alpha beta beta'gamma) was purified from wheat embryo. By the phosphorylation, EF-1 beta activity (GDP/GTP exchange activity) was stimulated. In contrast to these results, animal EF-1 delta which corresponds to plant EF-1 beta was inhibited by the phosphorylation. Interestingly, the phosphorylation sites on EF-1 beta and EF-1 delta are different.
In the course of these experiments, "simple method for analyzing phosphoamino acid by thin-layr chromatography" had been established, and the method was applied for the analysis of the phosphorylation of EF-1 from wheat embryo.
In the present research, "continuously coupled transcription-translation system for the production of rice cytoplasmic aldolase" had been established also.
|
