The structuer and function of the bacterial polypeptide elongation factors Tu and Ts are being studied by the methods of protein chemistry and enzyme kinetics to define the modes of action of the factors in molecular detail. With the aid of the recently determined primary structure of EF-Tu, the binding sites of guanosine nucleotides, EF-Ts, AA-tRNA, kirromycin and ribosomes will be identified and correlated on the three dimensional model of the protein that is now being constructed. To understand how GDP and GTP regulate the function of EF-Tu, differences between the reactivities of various residues in EF-Tu-GDP and EF-Tu-GTP will be explored. A kinetic analysis of the EF-Ts catalyzed reaction will be undertaken to clarify the mechanism of action of this protein.

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM030800-04
Application #
3278690
Study Section
(MG)
Project Start
1982-09-01
Project End
1987-06-30
Budget Start
1985-09-01
Budget End
1987-06-30
Support Year
4
Fiscal Year
1985
Total Cost
Indirect Cost
Name
Institute for Basic Research in Dev Disabil
Department
Type
DUNS #
167205090
City
Staten Island
State
NY
Country
United States
Zip Code
10314
Zhang, W; Espinoza, D; Hines, V et al. (1997) Characterization of beta-amyloid peptide precursor processing by the yeast Yap3 and Mkc7 proteases. Biochim Biophys Acta 1359:110-22
Hwang, Y W; Sanchez, A; Hwang, M C et al. (1997) The role of cysteinyl residues in the activity of bacterial elongation factor Ts, a guanosine nucleotide dissociation protein. Arch Biochem Biophys 348:157-62
Zhang, Y; Tao, J; Zhou, M et al. (1997) Elongation factor Ts of Chlamydia trachomatis: structure of the gene and properties of the protein. Arch Biochem Biophys 344:43-52
Hwang, Y W; Carter, M; Miller, D L (1992) The identification of a domain in Escherichia coli elongation factor Tu that interacts with elongation factor Ts. J Biol Chem 267:22198-205
Ogiso, Y; Gutierrez, L; Wrathall, L S et al. (1990) trans-Dominant suppressor mutations of the H-ras oncogene. Cell Growth Differ 1:217-24
Dell, V A; Miller, D L; Johnson, A E (1990) Effects of nucleotide- and aurodox-induced changes in elongation factor Tu conformation upon its interactions with aminoacyl transfer RNA. A fluorescence study. Biochemistry 29:1757-63
Janiak, F; Dell, V A; Abrahamson, J K et al. (1990) Fluorescence characterization of the interaction of various transfer RNA species with elongation factor Tu.GTP: evidence for a new functional role for elongation factor Tu in protein biosynthesis. Biochemistry 29:4268-77
Hwang, Y W; McCabe, P G; Innis, M A et al. (1989) Site-directed mutagenesis of the GDP binding domain of bacterial elongation factor Tu. Arch Biochem Biophys 274:394-403
Hwang, Y W; Sanchez, A; Miller, D L (1989) Mutagenesis of bacterial elongation factor Tu at lysine 136. A conserved amino acid in GTP regulatory proteins. J Biol Chem 264:8304-9
Bobin, S A; Currie, J R; Merz, P A et al. (1987) The comparative immunoreactivities of brain amyloids in Alzheimer's disease and scrapie. Acta Neuropathol 74:313-23

Showing the most recent 10 out of 13 publications