Results 261 to 270 of about 317,876 (306)
Some of the next articles are maybe not open access.
tRNAs and tRNA mimics as cornerstones of aminoacyl-tRNA synthetase regulations
Biochimie, 2005Structural 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 +2 more
openaire +2 more sources
Recognition of tRNA by aminoacyl tRNA synthetases
Journal of Molecular Biology, 1967A 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, 2010AbstractViruses 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, 2003Movement 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
1995Abstract 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
Biological Chemistry, 1999
AbstractHistidyl-tRNA synthetase (HisRS) is responsible for the synthesis of histidyl-transfer RNA, which is essential for the incorporation of histidine into proteins. This amino acid has uniquely moderate basic properties and is an important group in many catalytic functions of enzymes.A compilation of currently known primary structures of HisRS ...
W, Freist +4 more
openaire +2 more sources
AbstractHistidyl-tRNA synthetase (HisRS) is responsible for the synthesis of histidyl-transfer RNA, which is essential for the incorporation of histidine into proteins. This amino acid has uniquely moderate basic properties and is an important group in many catalytic functions of enzymes.A compilation of currently known primary structures of HisRS ...
W, Freist +4 more
openaire +2 more sources
Biochemistry and Cell Biology, 1995
Direct measurements of the rates of dissociation of dipeptidyl-tRNA from the ribosome show that hyperaccurate SmP and SmD ribosomes have unstable A-site binding of peptidyl-tRNA, while P-site binding is extremely stable in relation to the wild type.
M, Ehrenberg +5 more
openaire +2 more sources
Direct measurements of the rates of dissociation of dipeptidyl-tRNA from the ribosome show that hyperaccurate SmP and SmD ribosomes have unstable A-site binding of peptidyl-tRNA, while P-site binding is extremely stable in relation to the wild type.
M, Ehrenberg +5 more
openaire +2 more sources
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 ...
R, Rigler, W, Wintermeyer
openaire +2 more sources
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 ...
R, Rigler, W, Wintermeyer
openaire +2 more sources
Nature Chemical Biology, 2018
Fast, single-molecule tracking microscopy monitors transitions between mobile and ribosome-bound fluorescent tRNAs to achieve nucleotide-resolution measurements of translation rates in living cells.
Achillefs N, Kapanidis, Mathew, Stracy
openaire +2 more sources
Fast, single-molecule tracking microscopy monitors transitions between mobile and ribosome-bound fluorescent tRNAs to achieve nucleotide-resolution measurements of translation rates in living cells.
Achillefs N, Kapanidis, Mathew, Stracy
openaire +2 more sources
Journal of Biomolecular Structure and Dynamics, 2015
tRNAs are widely believed to segregate into two classes, I and II. Computational analysis of eukaryotic tRNA entries in Genomic tRNA Database, however, leads to new, albeit paradoxical, presence of more than a thousand class-I tRNAs with uncharacteristic long variable arms (V-arms), like in class-II.
Sanga, Mitra +4 more
openaire +2 more sources
tRNAs are widely believed to segregate into two classes, I and II. Computational analysis of eukaryotic tRNA entries in Genomic tRNA Database, however, leads to new, albeit paradoxical, presence of more than a thousand class-I tRNAs with uncharacteristic long variable arms (V-arms), like in class-II.
Sanga, Mitra +4 more
openaire +2 more sources

