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Utilization of selenocysteyl-tRNA[Ser]Sec and seryl-tRNA[Ser]Sec in protein synthesis.
J Biol Chem. 1994 Nov 25; 269(47):29739-45.JB

Abstract

The UGA selenocysteine (Sec) codon in glutathione peroxidase mRNA and in selenoprotein P and the UGA stop codon in rabbit beta-globin mRNA were employed to study the utilization of Sec-tRNA[Ser]Sec and Ser-tRNA[Ser]Sec in protein synthesis. In vitro Ser-tRNA[Ser]Sec served as a suppressor of the UGA Sec codon as well as the UGA stop codon, while Sec-tRNA[Ser]Sec did not. However, in vivo Sec-tRNA[Ser]Sec did donate Sec to glutathione peroxidase in Xenopus oocytes microinjected with glutathione peroxidase mRNA and Sec-tRNA. A ribosome binding assay was devised to investigate the interaction of aminoacyl-tRNA, rabbit reticulocyte ribosomes, and eukaryotic elongation factor 1 (eEF-1) in response to the appropriate trinucleoside diphosphate template. Ser-tRNA[Ser]Sec bound weakly to ribosomes in the presence of eEF-1 and UGA as compared to Phe-tRNA, Ser-tRNAIGA, and Met-tRNAm which bound more efficiently in the presence of eEF-1 and the appropriate template. No increase in the binding of Sec-tRNA[Ser]Sec was observed under the same conditions as Ser-tRNA[Ser]Sec. The ribosome binding studies substantiated the finding that Ser-tRNA[Ser]Sec serves as a suppressor of UGA codons in protein synthesis, but Sec-tRNA[Ser]Sec does not. In addition, these studies provide strong evidence that a specific elongation factor is required in mammalian cells for insertion of Sec into protein from Sec-tRNA[Ser]Sec.

Authors+Show Affiliations

Laboratory of Experimental Carcinogenesis, NCI, National Institutes of Health, Bethesda, Maryland 20892.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, U.S. Gov't, P.H.S.

Language

eng

PubMed ID

7961966

Citation

Jung, J E., et al. "Utilization of selenocysteyl-tRNA[Ser]Sec and seryl-tRNA[Ser]Sec in Protein Synthesis." The Journal of Biological Chemistry, vol. 269, no. 47, 1994, pp. 29739-45.
Jung JE, Karoor V, Sandbaken MG, et al. Utilization of selenocysteyl-tRNA[Ser]Sec and seryl-tRNA[Ser]Sec in protein synthesis. J Biol Chem. 1994;269(47):29739-45.
Jung, J. E., Karoor, V., Sandbaken, M. G., Lee, B. J., Ohama, T., Gesteland, R. F., Atkins, J. F., Mullenbach, G. T., Hill, K. E., & Wahba, A. J. (1994). Utilization of selenocysteyl-tRNA[Ser]Sec and seryl-tRNA[Ser]Sec in protein synthesis. The Journal of Biological Chemistry, 269(47), 29739-45.
Jung JE, et al. Utilization of selenocysteyl-tRNA[Ser]Sec and seryl-tRNA[Ser]Sec in Protein Synthesis. J Biol Chem. 1994 Nov 25;269(47):29739-45. PubMed PMID: 7961966.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Utilization of selenocysteyl-tRNA[Ser]Sec and seryl-tRNA[Ser]Sec in protein synthesis. A1 - Jung,J E, AU - Karoor,V, AU - Sandbaken,M G, AU - Lee,B J, AU - Ohama,T, AU - Gesteland,R F, AU - Atkins,J F, AU - Mullenbach,G T, AU - Hill,K E, AU - Wahba,A J, PY - 1994/11/25/pubmed PY - 1994/11/25/medline PY - 1994/11/25/entrez SP - 29739 EP - 45 JF - The Journal of biological chemistry JO - J. Biol. Chem. VL - 269 IS - 47 N2 - The UGA selenocysteine (Sec) codon in glutathione peroxidase mRNA and in selenoprotein P and the UGA stop codon in rabbit beta-globin mRNA were employed to study the utilization of Sec-tRNA[Ser]Sec and Ser-tRNA[Ser]Sec in protein synthesis. In vitro Ser-tRNA[Ser]Sec served as a suppressor of the UGA Sec codon as well as the UGA stop codon, while Sec-tRNA[Ser]Sec did not. However, in vivo Sec-tRNA[Ser]Sec did donate Sec to glutathione peroxidase in Xenopus oocytes microinjected with glutathione peroxidase mRNA and Sec-tRNA. A ribosome binding assay was devised to investigate the interaction of aminoacyl-tRNA, rabbit reticulocyte ribosomes, and eukaryotic elongation factor 1 (eEF-1) in response to the appropriate trinucleoside diphosphate template. Ser-tRNA[Ser]Sec bound weakly to ribosomes in the presence of eEF-1 and UGA as compared to Phe-tRNA, Ser-tRNAIGA, and Met-tRNAm which bound more efficiently in the presence of eEF-1 and the appropriate template. No increase in the binding of Sec-tRNA[Ser]Sec was observed under the same conditions as Ser-tRNA[Ser]Sec. The ribosome binding studies substantiated the finding that Ser-tRNA[Ser]Sec serves as a suppressor of UGA codons in protein synthesis, but Sec-tRNA[Ser]Sec does not. In addition, these studies provide strong evidence that a specific elongation factor is required in mammalian cells for insertion of Sec into protein from Sec-tRNA[Ser]Sec. SN - 0021-9258 UR - https://www.unboundmedicine.com/medline/citation/7961966/Utilization_of_selenocysteyl_tRNA[Ser]Sec_and_seryl_tRNA[Ser]Sec_in_protein_synthesis_ L2 - http://www.jbc.org/cgi/pmidlookup?view=long&pmid=7961966 DB - PRIME DP - Unbound Medicine ER -