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Problems with the transorientation hypothesis

Published online by Cambridge University Press:  06 September 2002

SCOTT M. STAGG ,
MIKEL VALLE ,
RAJENDRA K. AGRAWAL ,
JOACHIM FRANK  and
STEPHEN C. HARVEY
SCOTT M. STAGG
Affiliation:
Department of Biochemistry and Molecular Genetics, University of Alabama at Birmingham, Birmingham, AL 35294-0005, USA
MIKEL VALLE
Affiliation:
Howard Hughes Medical Institute, Health Research Inc., Wadsworth Center, New York State Department of Health Empire State Plaza, Albany, NY 12201-0509, USA
RAJENDRA K. AGRAWAL
Affiliation:
Department of Biomedical Sciences, State University of New York at Albany, Albany, New York 12203, USA Wadsworth Center, New York State Department of Health, Empire State Plaza, Albany, New York 12201-0509, USA
JOACHIM FRANK
Affiliation:
Howard Hughes Medical Institute, Health Research Inc., Wadsworth Center, New York State Department of Health Empire State Plaza, Albany, NY 12201-0509, USA Department of Biomedical Sciences, State University of New York at Albany, Albany, New York 12203, USA
STEPHEN C. HARVEY
Affiliation:
Department of Biochemistry and Molecular Genetics, University of Alabama at Birmingham, Birmingham, AL 35294-0005, USA

Extract

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A novel mechanism for the very first step in polypeptide elongation on the ribosome has recently been proposed by Simonson and Lake (2002). According to their transorientation hypothesis, the incoming aminoacyl-transfer RNA (aa-tRNA) initially binds to the messenger RNA (mRNA) with the anticodon stacked on the 5′ side of the anticodon loop; then, following GTP hydrolysis, the tRNA swings into the A-site by switching from the 5′-stacked conformation to the classic 3′-stacked geometry while maintaining Watson–Crick base pairing with the mRNA. There are several serious problems with this proposal.

Information

Type
LETTER TO THE EDITOR
Information
RNA , Volume 8 , Issue 9 , September 2002 , pp. 1093 - 1094
Copyright
2002 RNA Society