Abstract

The long term goal of this research work is to gain a better understanding of the molecular mechanism of regulation of protein synthesis initiation in red blood cells and the roles of different factors in this process. In this research, we plan to purify the peptide chain initiation factors from rabbit reticulocytes and study their precise roles in specific steps in peptide chain initiation. We will prepare antibodies against the homogeneous factors. Several peptide chain initiation factors such as Co-eIF-2B, Co-eIF-2C and sRF are complex proteins and are composed of multiple polypeptides. We plan to prepare monoclonal antibodies against the active polypeptide component(s) in these complex proteins. We will use the antibodies in studies of protein synthesis in reticulocyte lysates and also in preparations of immuno-affinity columns for further purification of the factors. We will also compare the characteristics of the peptide chain initiation factors and also the overall mechanism for peptide chain initiation in different eukaryotic cells such as rat liver and wheat germ.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM022079-13
Application #
3270900
Study Section
Biochemistry Study Section (BIO)
Project Start
1978-05-01
Project End
1990-06-30
Budget Start
1988-07-01
Budget End
1989-06-30
Support Year
13
Fiscal Year
1988
Total Cost
Indirect Cost

  Institution

Name
University of Nebraska Lincoln
Department
Type
Schools of Arts and Sciences
DUNS #
555456995
City
Lincoln
State
NE
Country
United States
Zip Code
68588

  Publications

Datta, B; Datta, R (1999) Induction of apoptosis due to lowering the level of eukaryotic initiation factor 2-associated protein, p67, from mammalian cells by antisense approach. Exp Cell Res 246:376-83
Datta, B; Datta, R; Mukherjee, S et al. (1999) Increased phosphorylation of eukaryotic initiation factor 2alpha at the G2/M boundary in human osteosarcoma cells correlates with deglycosylation of p67 and a decreased rate of protein synthesis. Exp Cell Res 250:223-30
Chatterjee, M; Chatterjee, N; Datta, R et al. (1998) Expression and activity of p67 are induced during heat shock. Biochem Biophys Res Commun 249:113-7
Zou, C; Zhang, Z; Wu, S et al. (1998) Molecular cloning and characterization of a rabbit eIF2C protein. Gene 211:187-94
Saha, D; Wu, S; Bose, A et al. (1997) Viral infection. II. Hemin induces overexpression of p67 as it partially prevents appearance of an active p67-deglycosylase in baculovirus-infected insect cells. Arch Biochem Biophys 342:373-82
Gupta, S; Wu, S; Chatterjee, N et al. (1995) Regulation of an eukaryotic initiation factor-2 (eIF-2) associated 67 kDa glycoprotein (p67) and its requirement in protein synthesis. Gene Expr 5:113-22
Parkhurst, K M; Hileman, R E; Saha, D et al. (1994) Thermodynamic characterization of the cooperativity of 40S complex formation during the initiation of eukaryotic protein synthesis. Biochemistry 33:15168-77
Chakraborty, A; Saha, D; Bose, A et al. (1994) Regulation of eIF-2 alpha-subunit phosphorylation in reticulocyte lysate. Biochemistry 33:6700-6
Hileman, R E; Parkhurst, K M; Gupta, N K et al. (1994) Synthesis and characterization of conjugates formed between periodate-oxidized ribonucleotides and amine-containing fluorophores. Bioconjug Chem 5:436-44
Chakraborty, A; Saha, D; Bose, A et al. (1994) Mechanism of action of an eukaryotic initiation factor-2 (eIF-2) associated 67 kDa glycoprotein (p67) and an eIF-2 kinase (dsI). Indian J Biochem Biophys 31:236-42

Showing the most recent 10 out of 24 publications