| pubmed-article:10993083 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10993083 | lifeskim:mentions | umls-concept:C0002520 | lld:lifeskim |
| pubmed-article:10993083 | lifeskim:mentions | umls-concept:C0597295 | lld:lifeskim |
| pubmed-article:10993083 | lifeskim:mentions | umls-concept:C0002482 | lld:lifeskim |
| pubmed-article:10993083 | lifeskim:mentions | umls-concept:C0271510 | lld:lifeskim |
| pubmed-article:10993083 | pubmed:issue | 6800 | lld:pubmed |
| pubmed-article:10993083 | pubmed:dateCreated | 2000-9-28 | lld:pubmed |
| pubmed-article:10993083 | pubmed:abstractText | The formation of aminoacyl-transfer RNA is a crucial step in ensuring the accuracy of protein synthesis. Despite the central importance of this process in all living organisms, it remains unknown how archaea and some bacteria synthesize Asn-tRNA and Gln-tRNA. These amide aminoacyl-tRNAs can be formed by the direct acylation of tRNA, catalysed by asparaginyl-tRNA synthetase and glutaminyl-tRNA synthetase, respectively. A separate, indirect pathway involves the formation of mis-acylated Asp-tRNA(Asn) or Glu-tRNA(Gln), and the subsequent amidation of these amino acids while they are bound to tRNA, which is catalysed by amidotransferases. Here we show that all archaea possess an archaea-specific heterodimeric amidotransferase (encoded by gatD and gatE) for Gln-tRNA formation. However, Asn-tRNA synthesis in archaea is divergent: some archaea use asparaginyl-tRNA synthetase, whereas others use a heterotrimeric amidotransferase (encoded by the gatA, gatB and gatC genes). Because bacteria primarily use transamidation, and the eukaryal cytoplasm uses glutaminyl-tRNA synthetase, it appears that the three domains use different mechanisms for Gln-tRNA synthesis; as such, this is the only known step in protein synthesis where all three domains have diverged. Closer inspection of the two amidotransferases reveals that each of them recruited a metabolic enzyme to aid its function; this provides direct evidence for a relationship between amino-acid metabolism and protein biosynthesis. | lld:pubmed |
| pubmed-article:10993083 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10993083 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10993083 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10993083 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10993083 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10993083 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:10993083 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10993083 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10993083 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10993083 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:10993083 | pubmed:issn | 0028-0836 | lld:pubmed |
| pubmed-article:10993083 | pubmed:author | pubmed-author:SöllDD | lld:pubmed |
| pubmed-article:10993083 | pubmed:author | pubmed-author:BeckerH DHD | lld:pubmed |
| pubmed-article:10993083 | pubmed:author | pubmed-author:ChangW ZWZ | lld:pubmed |
| pubmed-article:10993083 | pubmed:author | pubmed-author:TumbulaD LDL | lld:pubmed |
| pubmed-article:10993083 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10993083 | pubmed:day | 7 | lld:pubmed |
| pubmed-article:10993083 | pubmed:volume | 407 | lld:pubmed |
| pubmed-article:10993083 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10993083 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10993083 | pubmed:pagination | 106-10 | lld:pubmed |
| pubmed-article:10993083 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:10993083 | pubmed:meshHeading | pubmed-meshheading:10993083... | lld:pubmed |
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| pubmed-article:10993083 | pubmed:meshHeading | pubmed-meshheading:10993083... | lld:pubmed |
| pubmed-article:10993083 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:10993083 | pubmed:articleTitle | Domain-specific recruitment of amide amino acids for protein synthesis. | lld:pubmed |
| pubmed-article:10993083 | pubmed:affiliation | Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06520-8114, USA. | lld:pubmed |
| pubmed-article:10993083 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10993083 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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