Purification and properties of suppressor seryl‐tRNA:ATP phosphotransferase from bovine liver

Mizutani, Takaharu; Hashimoto, Atsushi

doi:10.1016/0014-5793(84)80342-7

Cited by 47 publications

(23 citation statements)

References 17 publications

(14 reference statements)

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“…The serine moiety en the tRNA is 0-phosphorylated by a kinase (Mizutani and Hashimoto, 1984) and the corresponding 0-phosphoseryl-tRNA has been implicated, in a number of studies, in the insertion of 0-Pserine into protein (for a review see Hatfield ef al., 1990). Recently, evidence has been published which demonstrates that this tRNA carries selenocysteine in vivo and thus may be the homologue of the E. coli seIC gene product (Lee et al, 1989).…”

Section: Biological Distribution and Evolutionmentioning

confidence: 99%

Selenocysteine: the 21st amino acid

Böck¹,

Forchhammer²,

Heider³

et al. 1991

Molecular Microbiology

633

381

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SummaryGreat excitement was elicited in the field of selenium biochemistry in 1986 by the parallel discoveries that the genes encoding the selenoproteins glutathione peroxidase and bacterial formate dehydrogenase each contain an in-frame TGA codon within their coding sequence. We now know that this codon directs the incorporation of selenium, in the form of selenocysteine, into these proteins. Working with the bacterial system has led to a rapid increase in our knowledge of selenocysteine biosynthesis and to the exciting discovery that this system can now be regarded as an expansion of the genetic code. The prerequisites for such a definition are co-translational insertion into the polypeptide chain and the occurrence of a tRNA molecule which carries selenocysteine. Both of these criteria are fulfilled and, moreover, tRNA^"'' even has its own special translation factor which delivers it to the translating ribosome. It is the aim of this article to review the events leading to the elucidation of selenocysteine as being the 21st amino acid.

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Section: Biological Distribution and Evolutionmentioning

confidence: 99%

Selenocysteine: the 21st amino acid

Böck¹,

Forchhammer²,

Heider³

et al. 1991

Molecular Microbiology

633

381

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“…The TGA codon within this gene corresponds to a selenocysteine moiety in the gene product. We have recently shown that a minor tRNA in mammalian tissues which recognized UGA in a ribosome binding assay and was identified as an opal suppressor seryl-tRNA (6) and phosphoseryl-tRNA (10,23) is actually a selenocysteyl-tRNA (18), which is now designated as selenocysteine tRNA [Ser]Sec. These studies provide evidence that tRNA [ser]sec has a twofold function of serving as a carrier molecule upon which selenocysteine is synthesized and as a direct donor of selenocysteine to protein (e.g., glutathione peroxidase) in response to specific UGA codons (18).…”

mentioning

confidence: 99%

Selenocysteine tRNA[Ser]Sec gene is ubiquitous within the animal kingdom.

Lee¹,

Rajagopalan²,

Kim³

et al. 1990

Mol. Cell. Biol.

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Recently, a mammalian tRNA which was previously designated as an opal suppressor seryl-tRNA and phosphoseryl-tRNA was shown to be a selenocysteyl-tRNA (B. J. Lee, P. J. Worland, J. N. Davis, T. C. Stadtman, and D. Hatfield, J. Biol. Chem. 264:9724-9727, 1989). Hence, this tRNA is now designated as selenocysteyl-tRNA[ISrlsJ, and its function is twofold, to serve as (i) a carrier molecule upon which selenocysteine is biosynthesized and (ii) as a donor of selenocysteine, which is the 21st naturally occurring amino acid of protein, to the nascent polypeptide chain in response to specffic UGA codons. In the present study, the selenocysteine tRNA gene was sequenced from Xenopus laevis, Drosophila melanogaster, and Caenorhabditis elegans. The tRNA product of this gene was also identified within the seryl-tRNA population of a number of higher and lower animals, and the human tRNA FSerlsJ gene was used as a probe to identify homologous sequences within genomic DNAs of organisms throughout the animal kingdom. The studies showed that the tRNA[SerJSec gene has undergone evolutionary change and that it is ubiquitous in the animal kingdom.Further, we conclude that selenocysteine-containing proteins, as well as the use of UGA as a codon for selenocysteine, are far more widespread in nature than previously thought.

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“…(vi) They differ in their primary sequences by several pyrimidine transitions including one in the wobble position of their anticodons (7), and these transitions must occur post-transcriptionally since both species are encoded by the same gene (9)(10)(11)(12). (vii) They are phosphorylated on their serine moiety by a kinase to form phosphoseryl-tRNA (7,13). The genes corresponding to the human (10), rabbit (11), chicken (9), and Xenopus (unpublished results) opal suppressor phosphoserine tRNAs have been isolated and sequenced.…”

mentioning

confidence: 99%

“…The fact that they read the termination codon UGA in protein synthesis (6,7) and are phosphorylated on their serine moiety (7,13) suggests that these tRNAs donate a modified amino acid directly to protein in response to specific UGA codons. A mRNA from Sindbis and from Middleburg viruses (19) and mouse glutathione peroxidase mRNAs (20) (21), which agrees with the possibility that the opal suppressor phosphoseryl-tRNA may be involved in the occurrence of selenocysteine in glutathione peroxidase.…”

mentioning

confidence: 99%

Unique pathway of expression of an opal suppressor phosphoserine tRNA.

Lee¹,

Peña²,

Tobian³

et al. 1987

Proc. Natl. Acad. Sci. U.S.A.

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An opal suppressor phosphoserine tRNA gene is present in single copy in the genomes of higher vertebrates. We have shown that the product of this gene functions as a suppressor in an in vitro assay, and we have proposed that it may donate a modified amino acid directly to protein in response to specific UGA codons. In this report, we show through in vitro and in vivo studies that the human and Xenopus opal suppressor phosphoserine tRNAs are synthesized by a pathway that is, to the best of our knowledge, unlike that of any known eukaryotic tRNA. The primary transcript of this gene does not contain a 5'-leader sequence; and, therefore, transcription of this suppressor is initiated at the first nucleotide within the coding sequence. The 5'-terminal triphosphate, present on the primary transcript, remains intact through 3'-terminal maturation and through subsequent transport of the tRNA to the cytoplasm. The unique biosynthetic pathway of this opal suppressor may underlie its distinctive role in eukaryotic cells.

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Purification and properties of suppressor seryl‐tRNA:ATP phosphotransferase from bovine liver

Cited by 47 publications

References 17 publications

Selenocysteine: the 21st amino acid

Selenocysteine: the 21st amino acid

Selenocysteine tRNA[Ser]Sec gene is ubiquitous within the animal kingdom.

Unique pathway of expression of an opal suppressor phosphoserine tRNA.

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