| pubmed-article:2531290 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2531290 | lifeskim:mentions | umls-concept:C0020792 | lld:lifeskim |
| pubmed-article:2531290 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:2531290 | lifeskim:mentions | umls-concept:C0074289 | lld:lifeskim |
| pubmed-article:2531290 | lifeskim:mentions | umls-concept:C0243126 | lld:lifeskim |
| pubmed-article:2531290 | lifeskim:mentions | umls-concept:C0597603 | lld:lifeskim |
| pubmed-article:2531290 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
| pubmed-article:2531290 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
| pubmed-article:2531290 | pubmed:issue | 6248 | lld:pubmed |
| pubmed-article:2531290 | pubmed:dateCreated | 1990-1-4 | lld:pubmed |
| pubmed-article:2531290 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2531290 | pubmed:abstractText | During the biosynthesis of selenoproteins in both prokaryotes and eukaryotes, selenocysteine is cotranslationally incorporated into the nascent polypeptide chain through a process directed by a UGA codon that normally functions as a stop codon. Recently, four genes have been identified whose products are required for selenocysteine incorporation in Escherichia coli. One of these genes, selC, codes for a novel transfer RNA species (tRNAUCA) that accepts serine and cotranslationally inserts selenocysteine by recognizing the specific UGA codon. The serine residue attached to this tRNA is converted to selenocysteine in a reaction dependent on functional selA and selD gene products. By contrast, the selB gene product (SELB) is not required until after selenocysteyl-tRNA biosynthesis. Here we present evidence indicating that SELB is a novel translation factor. The deduced amino-acid sequence of SELB exhibits extensive homology with the sequences of the translation initiation factor-2 (IF-2) and elongation factor Tu (EF-Tu). Furthermore, purified SELB protein binds guanine nucleotides in a 1:1 molar ratio and specifically complexes selenocysteyl-tRNAUCA, but does not interact with seryl-tRNAUCA. Thus, SELB could be an amino acid-specific elongation factor, replacing EF-Tu in a special translational step. | lld:pubmed |
| pubmed-article:2531290 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2531290 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2531290 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:2531290 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2531290 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2531290 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2531290 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2531290 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2531290 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2531290 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2531290 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2531290 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2531290 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:2531290 | pubmed:issn | 0028-0836 | lld:pubmed |
| pubmed-article:2531290 | pubmed:author | pubmed-author:DoveP WPW | lld:pubmed |
| pubmed-article:2531290 | pubmed:author | pubmed-author:ForchhammerKK | lld:pubmed |
| pubmed-article:2531290 | pubmed:author | pubmed-author:LeinfelderWW | lld:pubmed |
| pubmed-article:2531290 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2531290 | pubmed:day | 23 | lld:pubmed |
| pubmed-article:2531290 | pubmed:volume | 342 | lld:pubmed |
| pubmed-article:2531290 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2531290 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2531290 | pubmed:pagination | 453-6 | lld:pubmed |
| pubmed-article:2531290 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:2531290 | pubmed:meshHeading | pubmed-meshheading:2531290-... | lld:pubmed |
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| pubmed-article:2531290 | pubmed:meshHeading | pubmed-meshheading:2531290-... | lld:pubmed |
| pubmed-article:2531290 | pubmed:year | 1989 | lld:pubmed |
| pubmed-article:2531290 | pubmed:articleTitle | Identification of a novel translation factor necessary for the incorporation of selenocysteine into protein. | lld:pubmed |
| pubmed-article:2531290 | pubmed:affiliation | Lehrstuhl für Mikrobiologie der Universität, München, FRG. | lld:pubmed |
| pubmed-article:2531290 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2531290 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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