2 GTPS ARE CONSUMED ON EF-TU PER PEPTIDE-BOND IN POLY(PHE) SYNTHESIS,IN SPITE OF SWITCHING STOICHIOMETRY OF THE EF-TU-CENTER-DOT-AMINOACYL-TRANSFER-RNA COMPLEX WITH TEMPERATURE

Authors
DINCBAS V BILGIN N SCOBLE J EHRENBERG M
Citation
V. Dincbas et al., 2 GTPS ARE CONSUMED ON EF-TU PER PEPTIDE-BOND IN POLY(PHE) SYNTHESIS,IN SPITE OF SWITCHING STOICHIOMETRY OF THE EF-TU-CENTER-DOT-AMINOACYL-TRANSFER-RNA COMPLEX WITH TEMPERATURE, FEBS letters, 357(1), 1995, pp. 19-22
Citations number
14
Categorie Soggetti
Biophysics,Biology
Journal title
FEBS letters → ACNP
ISSN journal
00145793
Volume
357
Issue
1
Year of publication
1995
Pages
19 - 22
Database
ISI
SICI code
0014-5793(1995)357:1<19:2GACOE>2.0.ZU;2-S
Abstract
Recent observations indicate that the stoichiometry for the complex be tween EF-Tu(.)GTP and aminoacyl-tRNA (aa-tRNA) changes with temperatur e. At 37 degrees C two EF-Tu(.)GTPs bind one aa-tRNA in an extended te rnary complex, but at 0 degrees C the complex has 1:1 stoichiometry. H owever, the present experiments show that there are two GTPs hydrolyze d on EF-Tu per peptide bond in poly(Phe) synthesis at 37 degrees C as well as at 0 degrees C. This indicates two different pathways for the enzymatic binding of aa-tRNA to the A-site on the ribosome.