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Import of tRNAs and aminoacyl-tRNA synthetases into mitochondria
Current Genetics, 2008During evolution, most of the bacterial genes from the ancestral endosymbiotic alpha-proteobacteria at the origin of mitochondria have been either lost or transferred to the nuclear genome. A crucial evolutionary step was the establishment of macromolecule import systems to allow the come back of proteins and RNAs into the organelle. Paradoxically, the
Laurence Maréchal-Drouard +2 more
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Biochimie, 1976
The methylation of tRNA is a post-transcriptional modification which is achieved by specific enzymes, the tRNA methylases, with S adenosylmethionine as a methyl donor. The level and pattern of methylation are characteristic of the tRNA species and origin. Abnormally methylated tRNAs have been obtained, in vivo and in vitro, by a variety of methods, and
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The methylation of tRNA is a post-transcriptional modification which is achieved by specific enzymes, the tRNA methylases, with S adenosylmethionine as a methyl donor. The level and pattern of methylation are characteristic of the tRNA species and origin. Abnormally methylated tRNAs have been obtained, in vivo and in vitro, by a variety of methods, and
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Binding of Formylmethionyl-tRNA and Aminoacyl-tRNA to Ribosomes
Nature, 1968Inhibition of aminoacyl-tRNA binding by the purified initiation factors f1 and f2 could be regarded as a mechanism for ensuring that only F-met-tRNA binds initially to the entry site, thereby preventing random or non-specific binding by aminoacyl-tRNA.
Takahisa Ohta, Robert E. Thach
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The T-arm of tRNA is a substrate for tRNA (m5U54)-methyltransferase
Biochemistry, 1991Fragments of Escherichia coli FUra-tRNA(1Val) as small as 15 nucleotides form covalent complexes with tRNA (m5U54)-methyltransferase (RUMT). The sequence essential for binding includes position 52 of the T-stem and the T-loop and extends toward the 3' acceptor end of FUra-tRNA. The in vitro synthesized 17mer T-arm of E. coli tRNA(1Val), composed of the
Daniel V. Santi, Xiangrong Gu
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Recognition of tRNA by isoleucyl-tRNA synthetase
Journal of Molecular Biology, 1969Abstract An interaction between the isoleucine catalytic site and the tRNA recognition site of isoleucyl-tRNA synthetase (Escherichia coli) was detected using an assay for the binding of tRNA to enzyme. The effect of isoleucine is to increase the rate at which tRNA enters and leaves its binding site by sixfold without, therefore, a large effect on ...
Paul Berg, Michael Yarus
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The specificity of aminoacylation: a tRNA-tRNA interaction model
Journal of Theoretical Biology, 1978Abstract Most of the isoacceptor species for a particular tRNA can be classified according to the middle base in the anticodon together with the fourth base in the amino acid stem. These specifying nucleotides would operate if a tRNA-tRNA interaction occurs on the aminoacyl-tRNA synthetase so that the anticodon of one tRNA molecule faces the fourth ...
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Unexpected Functions of tRNA and tRNA Processing Enzymes
2011tRNA and tRNA processing enzymes impact more than protein production. Studies have uncovered roles for tRNA in the regulation of transcription, translation and protein turnover. Induced by stress or as a programmed part of development, nonrandom tRNA fragments can guide mRNA cleavage, inhibit translation and promote morphological changes.
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Reaction of Aminoacyl-tRNA Synthetases with Heterologous tRNA's
1971Publisher Summary This chapter reviews that the incorporation of an amino acid into a peptide chain involves, first, the reaction of the amino acid and ATP with a specific enzyme to form an enzyme complex with aminoacyl-adenylate (E. AA-AMP), and second, the reaction of this complex with a specific tRNA to form an ester of the amino acid with the 2'-
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On the Recognition of tRNA by Its Aminoacyl-tRNA Liqase
1971Publisher Summary This chapter reviews that experiments testing the adaptor hypothesis have shown conclusively that mRNA translation by aminoacyl-tRNA is independent of the amino acid attached to the tRNA. This means that esterification of the tRNA, catalyzed by its aminoacyl-tRNA ligase, must be specific if mistaken insertions of amino acids into ...
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