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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1991-10-24
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pubmed:abstractText |
The mechanisms of the synthesis of mammalian selenocysteyl-(Scy)-tRNA were studied using [75SE]H2Se. H2Se was prepared from [75Se]selenite, glutathione, NADPH and glutathione reductase, and was purified by chromatography. It was confirmed that this H2Se was a Se donor in the reaction of the synthesis of Scy-tRNA. [75Se]Scy, liberated from aminoacyl-tRNA, was analyzed by TLC on silica gel an subsequent autoradiography. The activity of Scy-tRNA synthesis was found in the supernatant at 105,000 x g of the murine liver extract, but not in the precipitate. The supernatant was chromatographed on DEAE-cellulose, and the activity was eluted at a concentration of 0.17 M KCl. This position is at the front shoulder of the peak of seryl-tRNA synthetase which was eluted at 0.20 M KCl. Major serine tRNA(IGA) is not a substrate on which to synthesize Scy-tRNA, but natural opal suppressor serine tRNA is. On a chromatographic pattern of a Scy-tRNA preparation on Sephacryl S-200, the radioactivity of 75Se was eluted at the tRNA peak. This showed that Scy bound to tRNA. The active protein fraction from DEAE-cellulose did not contain tRNA kinase, therefore Scy-tRNA must be directly synthesized from seryl-tRNA, not through phosphoseryl-tRNA. This mechanism is similar to that seen in Escherichia coli [1991, J. Biol. Chem. 266, 6324].
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Glutathione,
http://linkedlifedata.com/resource/pubmed/chemical/Glutathione Reductase,
http://linkedlifedata.com/resource/pubmed/chemical/NADP,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Transfer, Amino Acyl,
http://linkedlifedata.com/resource/pubmed/chemical/Selenium,
http://linkedlifedata.com/resource/pubmed/chemical/Selenium Radioisotopes,
http://linkedlifedata.com/resource/pubmed/chemical/selenocysteinyl-tRNA
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0014-5793
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
2
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pubmed:volume |
289
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
59-63
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:1894009-Animals,
pubmed-meshheading:1894009-Autoradiography,
pubmed-meshheading:1894009-Cattle,
pubmed-meshheading:1894009-Chromatography, DEAE-Cellulose,
pubmed-meshheading:1894009-Chromatography, Thin Layer,
pubmed-meshheading:1894009-Glutathione,
pubmed-meshheading:1894009-Glutathione Reductase,
pubmed-meshheading:1894009-Hydrolysis,
pubmed-meshheading:1894009-Liver,
pubmed-meshheading:1894009-NADP,
pubmed-meshheading:1894009-RNA, Transfer, Amino Acyl,
pubmed-meshheading:1894009-Selenium,
pubmed-meshheading:1894009-Selenium Radioisotopes
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pubmed:year |
1991
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pubmed:articleTitle |
Study of mammalian selenocysteyl-tRNA synthesis with [75Se]HSe.
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pubmed:affiliation |
Faculty of Pharmaceutical Sciences, Nagoya City University, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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