ArticleMolecular biology reports1998
The dual identities of mammalian tRNA(Sec) for SerRS and selenocysteine synthase.
Article in Molecular biology reports, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 13 citations in OpenAlex.
- Overcoming Challenges with Biochemical Studies of Selenocysteine and Selenoproteins.International journal of molecular sciences · 2024Review
- Naturally Occurring tRNAs With Non-canonical Structures.Frontiers in microbiology · 2020Review
- Insights into substrate promiscuity of human seryl-tRNA synthetase.RNA (New York, N.Y.) · 2017Article
- Transfer RNAs with novel cloverleaf structures.Nucleic acids research · 2017Article
- tRNA acceptor-stem and anticodon bases embed separate features of amino acid chemistry.RNA biology · 2016Article
- Active bovine selenophosphate synthetase 2, not having selenocysteine.Molecular biology reports · 2008Article
- pGp as the main product of bovine tRNA kinase.Molecular biology reports · 2002Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Se is an essential trace element and is found as a selenocysteine in the active site of Se-enzymes, such as glutathione peroxidase. tRNASec is first aminoacylated with serine by Ser RS and further is converted to selenocysteyl-tRNA by selenocysteine synthase. Mammalian selenocysteine tRNA has dual identities with Ser RS and selenocysteine synthase. Key identity elements for selenocysteine synthase are the long 9 bp AA- and long 6 bp D-stems. Major serine tRNA was converted to a mutant with a 9 bp AA-stem and 6 bp D-stem, instead of a 7 bp AA-stem and 3 bp D-stem. This mutant was active for selenylation as well as serylation. The relative kinetic parameter (Vmax/Km) of the mutant was 0.052 of the value (1.00) of wild-type Sec tRNA. This low value suggests that there is an unknown fine base specific for selenocysteine synthase. For serylation, mutant having 12 bp and wild type tRNASec having 13 bp of the total length of AA- + T-stems were active but the mutants having 11 or 14 bp were inactive. This shows that SerRS measures the distance between the discrimination base and long extra arm for recognition of tRNASer.
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