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tRNAs and tRNA mimics as cornerstones of aminoacyl-tRNA synthetase regulations

Biochimie, 2005
Structural plasticity of transfer RNA (tRNA) molecules is essential for interactions with their biological partners in aminoacylation reactions and during ribosome-dependent protein synthesis. This holds true when tRNAs are recruited for other functions than translation. Here we review regulation pathways where tRNAs and tRNA mimics play a pivotal role.
Magali Frugier   +2 more
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Recognition of tRNA by aminoacyl tRNA synthetases

Journal of Molecular Biology, 1967
A new method is described for the detection of tRNA in complex with an aminoacyl tRNA synthetase. Escherichia coli isoleucyl tRNA synthetase complexes only with tRNA Ile and tyrosyl tRNA synthetase complexes exclusively with tRNA Tyr . ATP and amino acid are not required to establish the complex, which also forms equally well whether the tRNA is ...
Michael Yarus, Paul Berg
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tRNA, tRNA Processing, and Aminoacyl-tRNA Synthetases

2014
This chapter provides an overview of tRNA, tRNA processing, and tRNA synthetases in Bacillus subtilis, emphasizing the areas in which there are distinct differences from Escherichia coli. It discusses the general characteristics of tRNA in the gram-positive bacteria. Despite the common belief that most bacteria are similar to E.
Christopher J. Green, Barbara S. Vold
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tRNA IDENTITY

Annual Review of Biochemistry, 1989
In the translation of genetic information from nucleic acid to protein, transfer RNA plays a crucial intermediate role. Each codon is read by a unique tRNA, which has been aminoacylated with the appropriate amino acid. Because of degeneracy in the genetic code there are, in general, more than one tRNA for each amino acid (1).
Normanly, Jennifer, Abelson, John
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Viral tRNAs and tRNA‐like structures

WIREs RNA, 2010
AbstractViruses commonly exploit or modify some aspect of tRNA biology. Large DNA viruses, especially bacteriophages, phycodnaviruses, and mimiviruses, produce their own tRNAs, apparently to adjust translational capacity during infection. Retroviruses recruit specific host tRNAs for use in priming the reverse transcription of their genome.
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tRNA mimics

Current Opinion in Structural Biology, 1998
Mimics recapitulating the structural features of tRNAs are involved in biological processes other than ribosome-dependent protein synthesis. A knowledge of the rules underlying the architecture and function of tRNAs allows the design of non-natural mimics.
R, Giegé, M, Frugier, J, Rudinger
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Dynamics of tRNA

Annual Review of Biophysics and Bioengineering, 1983
tRNA, because of its importance in gene translation, is widely studied. To date more than 200 primary structures are known (35), and the crystal structures of several tRNAs have been solved (61, 70, :83, 119, 120, 150, 154). From comparison of the nucleotide sequence aJ).d the tertiary structure of several tRNA species, features common to all tRNAs ...
W Wintermeyer, R Rigler
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Recognition of tRNAs by aminoacyl-tRNA synthetases.

The FASEB Journal, 1993
Our present understanding of the molecular mechanisms responsible for the recognition of tRNAs by their cognate aminoacyl-tRNA synthetases (aaRS) is essentially based on three sources of information: 1) the characterization of tRNA identity determinants using in vivo and in vitro approaches, 2) the classification of synthetases from primary sequence ...
Dino Moras, Jean Cavarelli
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tRNA hopping: effects of mutant tRNAs

Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression, 2003
Movement of tRNA and mRNA through the ribosome is coupled. However, selection for suppression of a -1 frameshift mutation in Escherichia coli has yielded a class of mutant tRNAs that can violate this mechanism and "hop" or disengage from their cognate codons and re-pair downstream in the mRNA.
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