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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
Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Cell and Molecular Biology.
1995 (English)In: FEBS LETTERS, ISSN 0014-5793, Vol. 357, no 1, 19-22 p.Article in journal (Other scientific) Published
Abstract [en]

Recent observations indicate that the stoichiometry for the complex between EF-Tu(.)GTP and aminoacyl-tRNA (aa-tRNA) changes with temperature. At 37 degrees C two EF-Tu(.)GTPs bind one aa-tRNA in an extended ternary complex, but at 0 degrees C the complex

Place, publisher, year, edition, pages
ELSEVIER SCIENCE BV , 1995. Vol. 357, no 1, 19-22 p.
Keyword [en]
GTP HYDROLYSIS; TRANSLATION; POLY(PHE) SYNTHESIS; ELONGATION FACTOR TU; TERNARY COMPLEX; TRANSFER-RNA-BINDING; ESCHERICHIA-COLI; MOLECULES PARTICIPATE; RIBOSOMES; ELONGATION
Identifiers
URN: urn:nbn:se:uu:diva-80621OAI: oai:DiVA.org:uu-80621DiVA: diva2:108535
Note
Addresses: BIOMED CTR, DEPT MOLEC BIOL, S-75124 UPPSALA, SWEDEN.Available from: 2008-10-17 Created: 2008-10-17 Last updated: 2011-01-15

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