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Aminoacylated tmRNA from Escherichia coli interacts with prokaryotic elongation factor Tu

Published online by Cambridge University Press:  07 July 2001

JOËLLE RUDINGER-THIRION
Affiliation:
Unité Propre de Recherche 9002 du Centre National de la Recherche Scientifique, Institut de Biologie Moléculaire et Cellulaire, F-67084 Strasbourg, France
RICHARD GIEGÉ
Affiliation:
Unité Propre de Recherche 9002 du Centre National de la Recherche Scientifique, Institut de Biologie Moléculaire et Cellulaire, F-67084 Strasbourg, France
BRICE FELDEN
Affiliation:
Department of Human Genetics, University of Utah, Salt Lake City, Utah 84112-5330, USA

Abstract

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Eubacterial tmRNAs (10Sa RNAs) are unique because they function, at least in Escherichia coli, both as tRNA and mRNA (for a review, see Muto et al., 1998). These ∼360 ± 40-nt-long RNAs are charged with alanine at their 3′ ends by alanyl-tRNA synthetases or AlaRS (Komine et al., 1994; Ushida et al., 1994). Alanylation occurs thanks to the presence of the equivalent of the G3-U70 pair, the major identity element for the alanylation of canonical tRNAs (Hou & Schimmel, 1988; McClain & Foss, 1988). Bacterial tmRNAs also have a short reading frame coding for 9 to 27 amino acids, depending on the species. E. coli tmRNA mediates recycling of ribosomes stalled at the end of terminatorless mRNAs, via a trans-translation process (Tu et al., 1995; Keiler et al., 1996; Himeno et al., 1997; Withey & Friedman, 1999). In E. coli, this amino acid tag is cotranslationally added to polypeptides synthesized from mRNAs lacking a termination codon, and the added 11-amino-acid C-terminal tag makes the protein a target for specific proteolysis (Keiler et al., 1996).

Type
LETTER TO THE EDITOR
Information
RNA , Volume 5 , Issue 8 , August 1999 , pp. 989 - 992
Copyright
1999 RNA Society
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