Abstract
Selenoproteins are proteins carrying the rare amino acid Sec (selenocysteine). Full expression of selenoproteins requires modification of tRNA([Ser]Sec), including N(6)-isopentenylation of base A(37). We show that Trit1 is a dimethylallyl:tRNA([Ser]Sec) transferase. Knockdown of Trit1 reduces expression of selenoproteins. Incubation of in vitro transcribed tRNA[Ser]Sec with recombinant Trit1 transfers [(14)C]dimethylallyl pyrophosphate to tRNA([Ser]Sec). 37A>G tRNA([Ser]Sec) is resistant to isopentenylation by Trit1.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Alkyl and Aryl Transferases / genetics*
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Alkyl and Aryl Transferases / metabolism
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Animals
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Base Sequence
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Hep G2 Cells
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Humans
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Mice
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Molecular Sequence Data
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NIH 3T3 Cells
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Nucleic Acid Conformation
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RNA, Transfer, Amino Acyl / genetics*
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RNA, Transfer, Amino Acyl / metabolism
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Selenoproteins / genetics*
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Selenoproteins / metabolism
Substances
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RNA, Transfer, Amino Acyl
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Selenoproteins
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selenocysteinyl-tRNA
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Alkyl and Aryl Transferases
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tRNA((Ser)Sec)-isopentenyl transferase, mouse