PMID: 7029532Sep 1, 1981Paper

Three tRNA binding sites on Escherichia coli ribosomes

Proceedings of the National Academy of Sciences of the United States of America
H J RheinbergerK H Nierhaus

Abstract

The binding of N-acetyl-Phe-tRNAPhe (an analogue of peptidyl-tRNA), Phe-tRNAPhe, and deacylated tRNAPhe to poly(U)-programmed tightly coupled 70S ribosomes was studied. The N-acetyl-Phe-tRNAPhe binding is governed by an exclusion principle: not more than one N-acetyl-Phe-tRNAPhe can be bound per ribosome, although this peptidyl-tRNA analogue can be present either at the aminoacyl-tRNA (A) site or the peptidyl-tRNA (P) site. Two Phe-tRNAPhe molecules are accepted by one ribosome in the presence of poly(U). This aminoacyl-tRNA binds enzymatically (in the presence of elongation factor Tu and GTP) and nonenzymatically to the A site and is then transferred to the P site, if that site is free. If this elongation factor G-independent movement is hampered, either by using an incubation temperature of 0 degrees C or by the addition of the translocation inhibitor viomycin, only one Phe-tRNAPhe per ribosome can be bound. The effect of the peptidyltransferase inhibitor chloramphenicol on the binding is similar to that of viomycin. In the absence of poly(U), Phe-tRNAPhe cannot bind to the ribosome. Deacylated [14C]tRNAPhe can bind in three copies to one ribosome. The new third tRNA binding site is called the "E" site. The sequence of fillin...Continue Reading

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Citations

May 1, 1994·Molecular Biology Reports·C G Proud
Apr 11, 1988·FEBS Letters·M V RodninaS V Kirillov
Jan 1, 1982·Progress in Biophysics and Molecular Biology·A Liljas
Jan 1, 1986·Progress in Biophysics and Molecular Biology·K Nagano, M Harel
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Jul 1, 1983·Proceedings of the National Academy of Sciences of the United States of America·H J Rheinberger, K H Nierhaus
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