Abstract

The role of phosphorylation in the regulation and maintenance of protein synthesis will be examined. Emphasis will be placed on the site-specific phosphorylation of initiation factor 2 (eIF-2), ribosomes and aminoacyl-tRNA synthetases. eIF-2, phosphorylated at 4 different sites by 3 different protein kinases, and 40S ribosomal subunits, phosphorylated at 4-5 sites on protein S6 by 3 different protein kinases and at 1 site on protein S10 by another protein kinase, will be examined in a reconstituted protein synthesizing system and in the various partial reactions of protein synthesis. We will examine the hemin requirement for maintenance of protein synthesis in reticulocytes using a hemin-affinity column to isolate the hemin-binding proteins. The aminoacyl-tRNA synthetases which are regulated by phosphorylation will be identified. Several enzymes of interest, including methionyl-tRNA synthetase, will be purified. These aminoacyl-tRNA synthetases will be examined at the molecular level to determine the role of phosphorylation in the regulation of activity.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM021424-11
Application #
3270471
Study Section
Molecular Biology Study Section (MBY)
Project Start
1977-07-01
Project End
1987-06-30
Budget Start
1985-09-01
Budget End
1987-06-30
Support Year
11
Fiscal Year
1985
Total Cost
Indirect Cost

  Institution

Name
University of California Riverside
Department
Type
Earth Sciences/Resources
DUNS #
City
Riverside
State
CA
Country
United States
Zip Code
92521

  Publications

Peters, H I; Chang, Y W; Traugh, J A (1995) Phosphorylation of elongation factor 1 (EF-1) by protein kinase C stimulates GDP/GTP-exchange activity. Eur J Biochem 234:550-6
Chen, C J; Traugh, J A (1995) Expression of recombinant elongation factor 1 beta from rabbit in Escherichia coli. Phosphorylation by casein kinase II. Biochim Biophys Acta 1264:303-11
Morley, S J; Traugh, J A (1993) Stimulation of translation in 3T3-L1 cells in response to insulin and phorbol ester is directly correlated with increased phosphate labelling of initiation factor (eIF-) 4F and ribosomal protein S6. Biochimie 75:985-9
Sheu, G T; Traugh, J A (1992) Nucleotide sequence of a rabbit cDNA encoding elongation factor 1 gamma. Nucleic Acids Res 20:5849
Smith, M R; Jaramillo, M; Tuazon, P T et al. (1991) Modulation of the mitogenic activity of eukaryotic translation initiation factor-4E by protein kinase C. New Biol 3:601-7
Morley, S J; Dever, T E; Etchison, D et al. (1991) Phosphorylation of eIF-4F by protein kinase C or multipotential S6 kinase stimulates protein synthesis at initiation. J Biol Chem 266:4669-72
Venema, R C; Peters, H I; Traugh, J A (1991) Phosphorylation of valyl-tRNA synthetase and elongation factor 1 in response to phorbol esters is associated with stimulation of both activities. J Biol Chem 266:11993-8
Venema, R C; Peters, H I; Traugh, J A (1991) Phosphorylation of elongation factor 1 (EF-1) and valyl-tRNA synthetase by protein kinase C and stimulation of EF-1 activity. J Biol Chem 266:12574-80
Venema, R C; Traugh, J A (1991) Protein kinase C phosphorylates glutamyl-tRNA synthetase in rabbit reticulocytes stimulated by tumor promoting phorbol esters. J Biol Chem 266:5298-302
Tuazon, P T; Morley, S J; Dever, T E et al. (1990) Association of initiation factor eIF-4E in a cap binding protein complex (eIF-4F) is critical for and enhances phosphorylation by protein kinase C. J Biol Chem 265:10617-21

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