| pubmed-article:2129559 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2129559 | lifeskim:mentions | umls-concept:C0014834 | lld:lifeskim |
| pubmed-article:2129559 | lifeskim:mentions | umls-concept:C0009015 | lld:lifeskim |
| pubmed-article:2129559 | lifeskim:mentions | umls-concept:C0017337 | lld:lifeskim |
| pubmed-article:2129559 | lifeskim:mentions | umls-concept:C0004022 | lld:lifeskim |
| pubmed-article:2129559 | lifeskim:mentions | umls-concept:C0024376 | lld:lifeskim |
| pubmed-article:2129559 | lifeskim:mentions | umls-concept:C0002518 | lld:lifeskim |
| pubmed-article:2129559 | lifeskim:mentions | umls-concept:C1334043 | lld:lifeskim |
| pubmed-article:2129559 | lifeskim:mentions | umls-concept:C2697616 | lld:lifeskim |
| pubmed-article:2129559 | pubmed:issue | 23 | lld:pubmed |
| pubmed-article:2129559 | pubmed:dateCreated | 1991-2-1 | lld:pubmed |
| pubmed-article:2129559 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2129559 | pubmed:abstractText | By screening of an Escherichia coli plasmidic library using antibodies against aspartyl-tRNA synthetase (AspRS) several clones were obtained containing aspS, the gene coding for AspRS. We report here the nucleotide sequence of aspS and the corresponding primary structure of the aspartyl-tRNA synthetase, a protein of 590 amino acid residues with a Mr 65,913, a value in close agreement with that observed for the purified protein. Primer extension analysis of the aspS mRNA using reverse transcriptase located its 5'-end at 94 nucleotides upstream of the translation initiation AUG; nuclease S1 analysis located the 3'-end at 126 nucleotides downstream of the stop codon UGA. Comparison of the DNA-derived protein sequence with known aminoacyl-tRNA sequences revealed important homologies with asparaginyl- and lysyl-tRNA synthetases from E.coli; more than 25% of their amino acid residues are identical, the homologies being distributed preferencially in the first part and the carboxy-terminal end of the molecule. Mutagenesis directed towards a consensus tetrapeptide (Gly-Leu-Asp-Arg) and the carboxy-terminal end showed that both domains could be implicated in catalysis as well as in ATP binding. | lld:pubmed |
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| pubmed-article:2129559 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2129559 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2129559 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:2129559 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2129559 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:2129559 | pubmed:issn | 0305-1048 | lld:pubmed |
| pubmed-article:2129559 | pubmed:author | pubmed-author:DirheimerGG | lld:pubmed |
| pubmed-article:2129559 | pubmed:author | pubmed-author:GangloffJJ | lld:pubmed |
| pubmed-article:2129559 | pubmed:author | pubmed-author:ErianiGG | lld:pubmed |
| pubmed-article:2129559 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2129559 | pubmed:day | 11 | lld:pubmed |
| pubmed-article:2129559 | pubmed:volume | 18 | lld:pubmed |
| pubmed-article:2129559 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2129559 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2129559 | pubmed:pagination | 7109-18 | lld:pubmed |
| pubmed-article:2129559 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:2129559 | pubmed:year | 1990 | lld:pubmed |
| pubmed-article:2129559 | pubmed:articleTitle | Aspartyl-tRNA synthetase from Escherichia coli: cloning and characterisation of the gene, homologies of its translated amino acid sequence with asparaginyl- and lysyl-tRNA synthetases. | lld:pubmed |
| pubmed-article:2129559 | pubmed:affiliation | Institut de Biologie Moléculaire et Cellulaire du CNRS, Strasbourg, France. | lld:pubmed |
| pubmed-article:2129559 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2129559 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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