Mutations in the NKXD consensus element indicate that GTP binds to the γ-subunit of translation initiation factor eIF2

Initiation factor eIF2 binds GTP and promotes the binding of methionyl-tRNA to ribosomes. Biochemical and sequence evidence suggests that the GTP might bind to either the β- or γ-subunit of eIF2. Mutations were made in the NKXD consensus elements found in both subunits and individual mutant forms we...

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Bibliographic Details
Published in:FEBS letters 1995-09, Vol.372 (2), p.249-252
Main Authors: Naranda, Tatjana, Sirangelo, Ivana, Fabbri, Bradon J., Hershey, John W.B.
Format: Article
Language:English
Subjects:
Base Sequence
Binding Sites - genetics
Cell Line
eIF2
GTP binding
Guanosine Triphosphate - metabolism
Humans
Molecular Sequence Data
Mutagenesis
Mutagenesis, Site-Directed
Peptide Initiation Factors - genetics
Peptide Initiation Factors - metabolism
Prokaryotic Initiation Factor-2
Protein synthesis
RNA, Messenger - analysis
Tetrahydrofolate Dehydrogenase - biosynthesis
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Summary:Initiation factor eIF2 binds GTP and promotes the binding of methionyl-tRNA to ribosomes. Biochemical and sequence evidence suggests that the GTP might bind to either the β- or γ-subunit of eIF2. Mutations were made in the NKXD consensus elements found in both subunits and individual mutant forms were overexpressed in transiently transfected COS-1 cells. The effect on the translational efficiency of a reporter mRNA for dihydrofolate reductase was monitored. Mutations in the γ-subunit cause severe repression of protein synthesis, whereas those in the β-subunit are only mildly inhibitory. The results support the view that GTP binds exclusively to the γ-subunit.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(95)00993-J