Abstract
Previously [de Haro, C., Datta, A & Ochoa, S. (1978) Proc. Natl. Acad. Sci. USA 75, 243--247] it was shown with initiation factors from Artemia salina embryos that the activity of the initiator methionyl-tRNA binding factor eIF-2 is stimulated by another factor (ESP, for eIF-2 stimulating protein) present, like eIF-2, in ribosomal salt washes. Incubation of eIF-2 with translational inhibitor from rabit reticulocytes, in the presence of ATP, abolished the ESP effect. At physiological concentrations eIF-2 was virtually inactive without ESP. These observations indicated that the translational inhibitor acts by converting eIF-2 to a form that is not stimulated by ESP. The same observations have now been made with eIF-2 and ESP from rabbit reticulocytes but, in this case, the dependence of eIF-2 activity on ESP is much more pronounced than with the A. salina factors. eIF-2 from reticulocytes interacts with ESP from A. salina and conversely.
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Selected References
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- Cherbas L., London I. M. On the mechanism of delayed inhibition of protein synthesis in heme-defecient rabbit reticulocyte lysates. Proc Natl Acad Sci U S A. 1976 Oct;73(10):3506–3510. doi: 10.1073/pnas.73.10.3506. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Dasgupta A., Majumdar A., George A. D., Gupta N. K. Protein synthesis in rabbit reticulocytes. XV. Isolation of a ribosomal protein factor (CO-EIE-1) which stimulates Met-tRNAfMet binding to EIF-1. Biochem Biophys Res Commun. 1976 Aug 23;71(4):1234–1241. doi: 10.1016/0006-291x(76)90786-5. [DOI] [PubMed] [Google Scholar]
- Farrell P. J., Balkow K., Hunt T., Jackson R. J., Trachsel H. Phosphorylation of initiation factor elF-2 and the control of reticulocyte protein synthesis. Cell. 1977 May;11(1):187–200. doi: 10.1016/0092-8674(77)90330-0. [DOI] [PubMed] [Google Scholar]
- Gross M., Mendelewski J. Additional evidence that the hemin-controlled translational repressor from rabbit reticulocytes is a protein kinase. Biochem Biophys Res Commun. 1977 Jan 24;74(2):559–569. doi: 10.1016/0006-291x(77)90340-0. [DOI] [PubMed] [Google Scholar]
- Kramer G., Cimadevilla J. M., Hardesty B. Specificity of the protein kinase activity associated with the hemin-controlled repressor of rabbit reticulocyte. Proc Natl Acad Sci U S A. 1976 Sep;73(9):3078–3082. doi: 10.1073/pnas.73.9.3078. [DOI] [PMC free article] [PubMed] [Google Scholar]
- LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
- Levin D., Ranu R. S., Ernst V., London I. M. Regulation of protein synthesis in reticulocyte lysates: phosphorylation of methionyl-tRNAf binding factor by protein kinase activity of translational inhibitor isolated from hemedeficient lysates. Proc Natl Acad Sci U S A. 1976 Sep;73(9):3112–3116. doi: 10.1073/pnas.73.9.3112. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Nombela C., Nombela N. A., Ochoa S., Safer B., Anderson W. F., Merrick W. C. Polypeptide chain initiation in eukaryotes: mechanism of formation of initiation complex. Proc Natl Acad Sci U S A. 1976 Feb;73(2):298–301. doi: 10.1073/pnas.73.2.298. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Trachsel H., Staehelin T. Binding and release of eukaryotic initiation factor eIF-2 and GTP during protein synthesis initiation. Proc Natl Acad Sci U S A. 1978 Jan;75(1):204–208. doi: 10.1073/pnas.75.1.204. [DOI] [PMC free article] [PubMed] [Google Scholar]
- de Haro C., Datta A., Ochoa S. Mode of action of the hemin-controlled inhibitor of protein synthesis. Proc Natl Acad Sci U S A. 1978 Jan;75(1):243–247. doi: 10.1073/pnas.75.1.243. [DOI] [PMC free article] [PubMed] [Google Scholar]