The overall objective of the proposed research is to further our understanding of the mechanism of protein biosynthesis, and study the role of the different factors required for the translation of messenger RNA. In addition, we are interested in determining which factors are responsible for the regulation of protein synthesis during encystment and development of Artemia embryos. In the following year our research aims include: a. An examination of the conformational changes of E. coli 30S and 50S ribosomal subunits following their interaction with chain initiation factor 3 and ribosomal protein S1. b. Both dormant and developing embryos of the brine shrimp Artemia contain two factors, Co-eIF-2(A) and Co-eIF-2(B), which stimulate eIF-2 activity. Direct complex formation between eIF-2 and these factors will be determined. The factors will also be examined for stimulating the release of eIF-2-GDP from the 40S ribosomal subunit and for recycling eIF-2. The function of these factors in relation to the activity of phosphorylated eIF-2 will be assayed. c. Isolation and characterization of chain initiation factor 3 from dormant and developing embryos of Artemia.

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM025451-06
Application #
3273031
Study Section
Molecular Biology Study Section (MBY)
Project Start
1978-09-01
Project End
1987-12-31
Budget Start
1985-01-01
Budget End
1985-12-31
Support Year
6
Fiscal Year
1985
Total Cost
Indirect Cost
Name
University of Mississippi Medical Center
Department
Type
Schools of Medicine
DUNS #
928824473
City
Jackson
State
MS
Country
United States
Zip Code
39216
Singh, L P; Denslow, N D; Wahba, A J (1996) The interaction of rabbit reticulocyte guanine nucleotide exchange factor eIF-2B with chain initiation factor 2: studies with N-ethylmaleimide and trypsin. Biochem Biophys Res Commun 223:604-11
Singh, L P; Denslow, N D; Wahba, A J (1996) Modulation of rabbit reticulocyte guanine nucleotide exchange factor activity by casein kinases 1 and 2 and glycogen synthase kinase 3. Biochemistry 35:3206-12
Aroor, A R; Singh, L P; Wahba, A J (1995) Hexamethylene bisacetamide-induced differentiation of Friend virus-transformed murine erythroleukemia cells is associated with parallel changes in casein kinase II and guanine nucleotide exchange factor activities. Exp Hematol 23:1204-11
Singh, L P; Wahba, A J (1995) Allosteric activation of rabbit reticulocyte guanine nucleotide exchange factor activity by sugar phosphates and inositol phosphates. Biochem Biophys Res Commun 217:616-23
Singh, L P; Aroor, A R; Wahba, A J (1995) Inhibition of rabbit reticulocyte guanine nucleotide exchange factor activity by heparin and its reversal by polyamines. Biochem Biophys Res Commun 212:1007-14
Aroor, A R; Denslow, N D; Singh, L P et al. (1994) Phosphorylation of rabbit reticulocyte guanine nucleotide exchange factor in vivo. Identification of putative casein kinase II phosphorylation sites. Biochemistry 33:3350-7
Singh, L P; Arorr, A R; Wahba, A J (1994) Phosphorylation of the guanine nucleotide exchange factor and eukaryotic initiation factor 2 by casein kinase II regulates guanine nucleotide binding and GDP/GTP exchange. Biochemistry 33:9152-7
Singh, L P; Aroor, A R; Wahba, A J (1994) Translational control of eukaryotic gene expression. Role of the guanine nucleotide exchange factor and chain initiation factor-2. Enzyme Protein 48:61-80
Jung, J E; Karoor, V; Sandbaken, M G et al. (1994) Utilization of selenocysteyl-tRNA[Ser]Sec and seryl-tRNA[Ser]Sec in protein synthesis. J Biol Chem 269:29739-45
Hille, M B; Dholakia, J N; Wahba, A et al. (1990) In-vivo and in-vitro evidence supporting co-regulation of translation in sea-urchin eggs by polypeptide initiation factors, pH optimization, and mRNAs. J Reprod Fertil Suppl 42:235-48

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