Abstract

I. Effects of phosphorylation on regulation of aminoacylation. A. Examine the effects of phosphorylation in vivo and in vitro on aminoacyl-tRNA synthetase activities including aminoacylation, tRNA binding, synthesis of Ap4A, and complex association/dissociation. B. Compare the sites phosphorylated in vivo in response to hormones/TPA to those phosphorylated in vitro with purified protein kinases. C. Analyze the site-specific phosphorylation of eight synthetases in the high molecular weight complex and threonyl-tRNA synthetase in response to hormones and the tumor promoting phorbol ester, TPA, In Reuber H35 rat hepatoma cells and reticulocytes. D. Examine the remaining synthetases to determine whether they are phosphorylated. Those of interest will be examined in detail as described in A-C. II. Examine the effects of the site-specific phosphorylation of S6 by the cAMP-dependent protein kinase and PAK II on regulation of protein synthesis. A. Examine the effects of the site-specific phosphorylation of S6 on protein synthesis in a reconstituted protein synthesizing system using selected messages. B. Examine the effects of phosphorylation of S6 on binding of mRNA, binding of aminoacyl-tRNA, and binding of met-tRNAi. C. Compare changes in the site-specific phosphorylation of S6 in response to various hormones/TPA with changes in protein synthesis.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
2R01GM021424-12A1
Application #
3270467
Study Section
Physiological Chemistry Study Section (PC)
Project Start
1977-07-01
Project End
1992-06-30
Budget Start
1987-07-01
Budget End
1988-06-30
Support Year
12
Fiscal Year
1987
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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