PMID- 7961966
OWN - NLM
STAT- MEDLINE
DCOM- 19941228
LR  - 20210212
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 269
IP  - 47
DP  - 1994 Nov 25
TI  - Utilization of selenocysteyl-tRNA[Ser]Sec and seryl-tRNA[Ser]Sec in protein 
      synthesis.
PG  - 29739-45
AB  - 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.
FAU - Jung, J E
AU  - Jung JE
AD  - Laboratory of Experimental Carcinogenesis, NCI, National Institutes of Health, 
      Bethesda, Maryland 20892.
FAU - Karoor, V
AU  - Karoor V
FAU - Sandbaken, M G
AU  - Sandbaken MG
FAU - Lee, B J
AU  - Lee BJ
FAU - Ohama, T
AU  - Ohama T
FAU - Gesteland, R F
AU  - Gesteland RF
FAU - Atkins, J F
AU  - Atkins JF
FAU - Mullenbach, G T
AU  - Mullenbach GT
FAU - Hill, K E
AU  - Hill KE
FAU - Wahba, A J
AU  - Wahba AJ
AU  - et al.
LA  - eng
GR  - ES02497/ES/NIEHS NIH HHS/United States
GR  - GM25451/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Codon)
RN  - 0 (RNA, Transfer, Amino Acyl)
RN  - 0 (selenocysteinyl-tRNA)
RN  - EC 1.11.1.9 (Glutathione Peroxidase)
SB  - IM
MH  - Acylation
MH  - Animals
MH  - Codon
MH  - Glutathione Peroxidase/metabolism
MH  - Mutation
MH  - *Protein Biosynthesis
MH  - RNA, Transfer, Amino Acyl/*metabolism
MH  - Rabbits
MH  - Ribosomes/metabolism
EDAT- 1994/11/25 00:00
MHDA- 1994/11/25 00:01
CRDT- 1994/11/25 00:00
PHST- 1994/11/25 00:00 [pubmed]
PHST- 1994/11/25 00:01 [medline]
PHST- 1994/11/25 00:00 [entrez]
AID - S0021-9258(18)43943-9 [pii]
PST - ppublish
SO  - J Biol Chem. 1994 Nov 25;269(47):29739-45.