PMID:17483465: Difference between revisions
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| | !align=left |Citation | ||
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'''Rubio, MA, Pastar, I, Gaston, KW, Ragone, FL, Janzen, CJ, Cross, GA, Papavasiliou, FN and Alfonzo, JD''' (2007) An adenosine-to-inosine tRNA-editing enzyme that can perform C-to-U deamination of DNA. ''Proc. Natl. Acad. Sci. U.S.A.'' '''104''':7821-6 | |||
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!align=left |Abstract | |||
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Adenosine-to-inosine editing in the anticodon of tRNAs is essential for viability. Enzymes mediating tRNA adenosine deamination in bacteria and yeast contain cytidine deaminase-conserved motifs, suggesting an evolutionary link between the two reactions. In trypanosomatids, tRNAs undergo both cytidine-to-uridine and adenosine-to-inosine editing, but the relationship between the two reactions is unclear. Here we show that down-regulation of the Trypanosoma brucei tRNA-editing enzyme by RNAi leads to a reduction in both C-to-U and A-to-I editing of tRNA in vivo. Surprisingly, in vitro, this enzyme can mediate A-to-I editing of tRNA and C-to-U deamination of ssDNA but not both in either substrate. The ability to use both DNA and RNA provides a model for a multispecificity editing enzyme. Notably, the ability of a single enzyme to perform two different deamination reactions also suggests that this enzyme still maintains specificities that would have been found in the ancestor deaminase, providing a first line of evidence for the evolution of editing deaminases. | |||
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=17483465 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1876531 PMC1876531] | |||
Online version:[http://dx.doi.org/10.1073/pnas.0702394104 10.1073/pnas.0702394104] | |||
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|{{ | !align=left |Keywords | ||
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Adenosine/metabolism; Adenosine Deaminase/physiology; Amino Acid Sequence; Base Sequence; Cell Line; Cytidine/metabolism; Cytidine Deaminase/physiology; Deamination; Inosine/metabolism; Molecular Sequence Data; RNA Editing; RNA Interference; Uridine/metabolism | |||
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==Significance {{HelpIcon|Help:Literature}} == | ==Significance {{HelpIcon|Help:Literature}} == | ||
{{LitSignificance}} | {{LitSignificance}} | ||
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==Annotations {{HelpIcon|Help:Literature}}== | ==Annotations {{HelpIcon|Help:Literature}}== | ||
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==EcoliWiki Links {{HelpIcon|Help:Literature}} == | ==EcoliWiki Links {{HelpIcon|Help:Literature}} == | ||
Latest revision as of 04:31, 15 September 2013
| Citation |
Rubio, MA, Pastar, I, Gaston, KW, Ragone, FL, Janzen, CJ, Cross, GA, Papavasiliou, FN and Alfonzo, JD (2007) An adenosine-to-inosine tRNA-editing enzyme that can perform C-to-U deamination of DNA. Proc. Natl. Acad. Sci. U.S.A. 104:7821-6 |
|---|---|
| Abstract |
Adenosine-to-inosine editing in the anticodon of tRNAs is essential for viability. Enzymes mediating tRNA adenosine deamination in bacteria and yeast contain cytidine deaminase-conserved motifs, suggesting an evolutionary link between the two reactions. In trypanosomatids, tRNAs undergo both cytidine-to-uridine and adenosine-to-inosine editing, but the relationship between the two reactions is unclear. Here we show that down-regulation of the Trypanosoma brucei tRNA-editing enzyme by RNAi leads to a reduction in both C-to-U and A-to-I editing of tRNA in vivo. Surprisingly, in vitro, this enzyme can mediate A-to-I editing of tRNA and C-to-U deamination of ssDNA but not both in either substrate. The ability to use both DNA and RNA provides a model for a multispecificity editing enzyme. Notably, the ability of a single enzyme to perform two different deamination reactions also suggests that this enzyme still maintains specificities that would have been found in the ancestor deaminase, providing a first line of evidence for the evolution of editing deaminases. |
| Links |
PubMed PMC1876531 Online version:10.1073/pnas.0702394104 |
| Keywords |
Adenosine/metabolism; Adenosine Deaminase/physiology; Amino Acid Sequence; Base Sequence; Cell Line; Cytidine/metabolism; Cytidine Deaminase/physiology; Deamination; Inosine/metabolism; Molecular Sequence Data; RNA Editing; RNA Interference; Uridine/metabolism |
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