The detection of natural opal suppressor seryl‐tRNA in <i>Escherichia coli</i> by the dot blot hybridization and its phosphorylation by a tRNA kinase

Mizutani, Takaharu; Maruyama, Naosuke; Hitaka, Teruaki; Sukenaga, Yoshikazu

doi:10.1016/0014-5793(89)81367-5

Cited by 14 publications

(5 citation statements)

References 17 publications

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“…The modification patterns of the hybrids at the low Na+ concentration (lanes [4][5][6][7][8] were mostly similar to those at the high Na+ concentration. A62, A64, A66 and A67 became more intensely modified in the hybrid with A4 (lane 4 and 6).…”

Section: Characterization Of the Hybridized Statementioning

confidence: 87%

“…In this regard, we have already reported specific and quantitative detection of a single tRNA species by a filter hybridization method, and the purification of some mitochondrial tRNAs by fusing this sensitive assay system and conventional open column chromatography [3,4]. This system was also used by others in order to quantitatively detect cellular suppressor serine tRNAs in dystrophic mouse muscle and in E. coli [7,8]. However, in the course of applying this procedure to other mitochondrial and nonmitochondrial tRNAs, some oligodeoxyribonucleotide probes were found not to hybridize to the corresponding tRNA species.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Effect of the higher-order structure of tRNAs on the stability of hybrids with oligodeoxyribonucleotides: separation of tRNA by an efficient solution hybridization

Kumazawa

Yokogawa²,

Tsurui

et al. 1992

Nucl Acids Res

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Section: Characterization Of the Hybridized Statementioning

confidence: 87%

Section: Introductionmentioning

confidence: 99%

Effect of the higher-order structure of tRNAs on the stability of hybrids with oligodeoxyribonucleotides: separation of tRNA by an efficient solution hybridization

Kumazawa

Yokogawa²,

Tsurui

et al. 1992

Nucl Acids Res

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“…After activation at the hydroxyl group, the leaving group is replaced by a selenol moiety to yield selenocysteinyl-tRNAUe6A. In eukaryotes, it has been unequivocally demonstrated that the active serine derivative is 03-phosphoseryl-tRNA (28,29); the evidence presented by Mizutani et al (30) that E. coli selenocysteine formation also involves O-phosphorylation of L-serine is less compelling.…”

Section: Discussionmentioning

confidence: 98%

“…Experiments have yet to be presented which show that (i) the in vitro phosphorylation reaction is dependent on the presence of the selC-encoded tRNA and (ii) the phosphorylated product is identical with O-phosphoserine ester-bonded to tRNA (30).…”

Section: Discussionmentioning

confidence: 99%

In vitro synthesis of selenocysteinyl-tRNA(UCA) from seryl-tRNA(UCA): involvement and characterization of the selD gene product.

Leinfelder¹,

Forchhammer²,

Veprek³

et al. 1990

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

173

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The selD gene from Escherichia coli, whose product is involved in selenium metabolism, has been cloned and sequenced. selD codes for a protein of 347 amino acids with a calculated molecular weight of 36,687. Analysis of the selD gene product through expression of the gene in the phage T7 promoter/polymerase system confirmed the predicted molecular weight of the protein. Gene disruption experiments demonstrated that the SelD protein is required both for the incorporation of selenium into the modified nucleoside 5-methylaminomethyl-2-selenouridine of tRNA and for the biosynthesis of selenocysteine from an L-serine residue esterbonded to tRNASe A. tRNASeA has been purified, aminoacylated with L-serine, and used as a substrate for the development of an in vitro system for selenocysteine biosynthesis. Efficient formation of selenocysteinyl-tRNAsA was achieved by using extracts in which both the selD and the selA gene products were overproduced. The results demonstrate that selenocysteine is synthesized from L-serine bound to tRNAUCA and they are in accord with SelD functioning as a donor of reduced selenium.

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“…The minor phosphoseryl-tRNA and another minor seryl-tRNA identified in bovine, rabbit, and chicken livers that decoded the stop codon UGA (12) were shown to be Sec tRNA [Ser]Sec (13). It was subsequently reported that phosphoseryl-tRNA [Ser]Sec was the intermediate in the biosynthesis of Sec in mammals (21,22) and in bacteria (23). However, after the identification of aminoacryltRNA [ (26).…”

Section: Discussionmentioning

confidence: 99%

Identification and characterization of phosphoseryl-tRNA ^[Ser]Sec kinase

Carlson

Kryukov

et al. 2004

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

174

187

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In 1970, a kinase activity that phosphorylated a minor species of seryl-tRNA to form phosphoseryl-tRNA was found in rooster liver [Maenpaa, P. H. & Bernfield, M. R. (1970) Proc. Natl. Acad. Sci. USA 67, 688 -695], and a minor seryl-tRNA that decoded the nonsense UGA was detected in bovine liver. The phosphoseryl-tRNA and the minor UGA-decoding seryl-tRNA were subsequently identified as selenocysteine (Sec) tRNA [Ser]Sec , but the kinase activity remained elusive. Herein, by using a comparative genomics approach that searched completely sequenced archaeal genomes for a kinase-like protein with a pattern of occurrence similar to that of components of Sec insertion machinery, we detected a candidate gene for mammalian phosphoseryl-tRNA [ S elenocysteine (Sec) has its own code word, UGA, and its own tRNA, and therefore is viewed as the 21st amino acid in the genetic code (reviewed in refs. 1-4). Although UGA usually codes for the termination of protein synthesis, it also specifies Sec if specific requirements are met. The presence of a stemloop structure downstream of UGA, called a Sec insertion sequence (SECIS) element, is the critical component in selenoprotein mRNAs that dictates UGA to code for Sec (reviewed in ref. 5). In mammals, the SECIS element occurs in the 3Ј untranslated region of selenoprotein mRNAs. A specific elongation factor, EFsec, specifically recognizes selenocysteyltRNA [Ser]Sec (6, 7), and a SECIS element binding protein, SBP2, binds specifically to the SECIS element (8), directing the insertion of Sec into protein in response to UGA.It has been known for several years that the biosynthesis of Sec occurs on its tRNA in both bacteria (9) and mammals (10) after the tRNA is initially aminoacylated with serine by seryl-tRNA synthetase. In Escherichia coli, the pathway for the biosynthesis of Sec has been completely established (reviewed in ref. 1). After the aminoacylation of bacterial tRNA [Ser]Sec with serine, the hydroxyl group is removed from the seryl moiety to yield an aminoacrylyl intermediate, and this step is catalyzed by a pyridoxal phosphate-dependent Sec synthase. The aminoacrylyl intermediate serves as the acceptor for the activated selenium donor, monoselenophosphate, which is synthesized from selenite and ATP in the presence of selenophosphate synthetase (reviewed in ref. 1). Once selenium is donated to the intermediate, the biosynthesis of Sec on tRNA [Ser]Sec is complete.In eukaryotes, however, the biosynthesis of Sec has not been established, but several components have been identified over the years that play a role in this process. For example, in 1970, a minor seryl-tRNA was reported to form phosphoseryl-tRNA by a kinase activity from rooster liver (11), and a minor seryl-tRNA from bovine, rabbit, and chicken livers was reported to specifically decode the nonsense codon UGA (12). Although it was subsequently shown that both the minor seryl-tRNA that formed phosphoseryl-tRNA and the one that decoded UGA were the same tRNA (13), it was not known at the time these components were ...

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The detection of natural opal suppressor seryl‐tRNA in Escherichia coli by the dot blot hybridization and its phosphorylation by a tRNA kinase

Cited by 14 publications

References 17 publications

Effect of the higher-order structure of tRNAs on the stability of hybrids with oligodeoxyribonucleotides: separation of tRNA by an efficient solution hybridization

Effect of the higher-order structure of tRNAs on the stability of hybrids with oligodeoxyribonucleotides: separation of tRNA by an efficient solution hybridization

In vitro synthesis of selenocysteinyl-tRNA(UCA) from seryl-tRNA(UCA): involvement and characterization of the selD gene product.

Identification and characterization of phosphoseryl-tRNA ^[Ser]Sec kinase

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The detection of natural opal suppressor seryl‐tRNA in Escherichia coli by the dot blot hybridization and its phosphorylation by a tRNA kinase

Cited by 14 publications

References 17 publications

Effect of the higher-order structure of tRNAs on the stability of hybrids with oligodeoxyribonucleotides: separation of tRNA by an efficient solution hybridization

Effect of the higher-order structure of tRNAs on the stability of hybrids with oligodeoxyribonucleotides: separation of tRNA by an efficient solution hybridization

In vitro synthesis of selenocysteinyl-tRNA(UCA) from seryl-tRNA(UCA): involvement and characterization of the selD gene product.

Identification and characterization of phosphoseryl-tRNA [Ser]Sec kinase

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Identification and characterization of phosphoseryl-tRNA ^[Ser]Sec kinase