Evidence for the formation of an unusual ternary complex of rabbit liver EF-1alpha with GDP and deacylated tRNA.
Eukaryotic translation elongation factor 1alpha is known to interact in GTP-bound form with aminoacyl-tRNA promoting its binding to the ribosome. In this paper another ternary complex [EF-1alpha*GDP*deacylated tRNA], never considered in widely accepted elongation schemes, is reported for the first time. The formation of this unusual complex, postulated earlier (FEBS Lett. (1996) 382, 18-20), has been detected by four independent methods. [EF-1alpha*GDP]-interacting sites are located in the acceptor stem, TpsiC stem and TpsiC loop of tRNA(Phe) and tRNA(Leu) molecules. Both tRNA and EF-1alpha are found to undergo certain conformational changes during their interaction. The ability of EF-1alpha to form a complex with deacylated tRNA indicates that the factor may perform an important role in tRNA and aminoacyl-tRNA channeling in higher eukaryotic cells.
Petrushenko
Z M
ZM
Institute of Molecular Biology and Genetics, National Academy of Sciences of Ukraine, Kiev.
Negrutskii
B S
BS
Ladokhin
A S
AS
Budkevich
T V
TV
Shalak
V F
VF
El'skaya
A V
AV
D000818:Animals; D001483:Base Sequence; D001665:Binding Sites; D005453:Fluorescence; D006153:Guanosine Diphosphate / Q000378:metabolism*; D008099:Liver / Q000378:metabolism*; D008969:Molecular Sequence Data; D009690:Nucleic Acid Conformation; D020648:Peptide Elongation Factor 1; D010445:Peptide Elongation Factors / Q000378:metabolism*; D014176:Protein Biosynthesis; D012343:RNA, Transfer / Q000378:metabolism*; D012356:RNA, Transfer, Leu / Q000378:metabolism; D012360:RNA, Transfer, Phe / Q000378:metabolism; D011817:Rabbits; D012261:Ribonucleoproteins / Q000378:metabolism*; D014364:Tryptophan / Q000737:chemistry
D020648:Peptide Elongation Factor 1; D010445:Peptide Elongation Factors; D012356:RNA, Transfer, Leu; D012360:RNA, Transfer, Phe; D012261:Ribonucleoproteins; D006153:Guanosine Diphosphate; D014364:Tryptophan; D012343:RNA, Transfer