Results 301 to 310 of about 345,668 (351)

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
openaire   +3 more sources

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
openaire   +2 more sources

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
openaire   +1 more source

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.
Michaël, Ryckelynck, Richard, Giegé, Magali, Frugier   +2 more
openaire   +2 more sources

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 ...
M, Yarus, P, Berg
openaire   +2 more sources

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.
openaire   +2 more sources

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.
openaire   +2 more sources

Atninoacyl-tRNA synthetase-tRNA recognition

1995
Abstract Aminoacylation is the first and key step in the translation of genetic messages into proteins. The reaction brings together amino acids and their cognate tRNAs and is catalysed by aminoacyl-tRNA synthetases (aaRSs). In the reaction the amino acid is esterified to one of the hydroxyl groups of the 3'-terminal adenosine; the ...
John G Arnez, Dino Moras
openaire   +1 more source