A pseudoknotted tRNA variant is a substrate for tRNA (cytosine-5)-methyltransferase from Xenopus laevis
Identifieur interne : 000294 ( France/Analysis ); précédent : 000293; suivant : 000295A pseudoknotted tRNA variant is a substrate for tRNA (cytosine-5)-methyltransferase from Xenopus laevis
Auteurs : Hervé Brulé [France] ; Henri Grosjean [France] ; Richard Giegé [France] ; Catherine Florentz [France]Source :
- Biochimie [ 0300-9084 ] ; 1998.
English descriptors
- KwdEn :
- Teeft :
- Acceptor, Acceptor branch, Anticodon, Biochimie, Canonical, Canonical trnas, Coli, Denaturing polyacrylamide, Elution solution, Enzymatic formation, Enzyme, Eukaryotic trna, Gieg6, Grosjean, Laevis, Methylation, Microinjected, Modification, Modification pattern, Mosaic, Mosaic virus, Nuclease, Nucleic, Nucleic acids, Nucleotide, Oocyte, Potential target nucleotides, Press washington, Rna, Rnase, Structural features, Transcript, Trna, Turnip, Tymv, Tymv domain, Tymv structure, Viral, Xenopus, Xenopus laevis, Xenopus laevis oocyte, Xenopus laevis oocytes, Xenopus oocytes, Yeast, Yeast trna, Yeast trnas.
Abstract
Abstract: tRNA post-transcriptional modification enzymes of Xenopus laevis were proposed previously to belong to two major groups according to their sensitivity to structural perturbations in their substrates. To further investigate the structural variations tolerated by these enzymes, the tRNA-like domain of turnip yellow mosaic virus RNA (88 nucleotides in length) has been microinjected into the oocytes of Xenopus laevis. This RNA possesses 12 potential target nucleotides for modification within a structure including a pseudoknotted folding, an extended anticodon stem, and unusual D-loop/T-loop interactions. Results indicate that only cytosine-42, a position equivalent to C-49 in canonical tRNAs, was quantitatively modified into m5C in the microinjected RNA. Modification was detected to high levels, indicating that at least one enzyme tolerates non-canonical structural features.
Url:
DOI: 10.1016/S0300-9084(99)80003-0
Affiliations:
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<front><div type="abstract" xml:lang="en">Abstract: tRNA post-transcriptional modification enzymes of Xenopus laevis were proposed previously to belong to two major groups according to their sensitivity to structural perturbations in their substrates. To further investigate the structural variations tolerated by these enzymes, the tRNA-like domain of turnip yellow mosaic virus RNA (88 nucleotides in length) has been microinjected into the oocytes of Xenopus laevis. This RNA possesses 12 potential target nucleotides for modification within a structure including a pseudoknotted folding, an extended anticodon stem, and unusual D-loop/T-loop interactions. Results indicate that only cytosine-42, a position equivalent to C-49 in canonical tRNAs, was quantitatively modified into m5C in the microinjected RNA. Modification was detected to high levels, indicating that at least one enzyme tolerates non-canonical structural features.</div>
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