rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
23
|
pubmed:dateCreated |
1991-2-1
|
pubmed:databankReference |
|
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.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/2129559-2183178,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2129559-2479982,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2129559-2642907,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2129559-2647492,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2129559-265521,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2129559-2668951,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2129559-2674137,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2129559-2693216,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2129559-271968,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2129559-2997739,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2129559-3047397,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2129559-3118944,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2129559-3275660,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2129559-3298660,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2129559-3304131,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2129559-342244,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2129559-3442641,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2129559-3474623,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2129559-3513127,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2129559-3545179,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2129559-382994,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2129559-3865201,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2129559-388356,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2129559-3888626,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2129559-3913464,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2129559-3991809,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/2129559-7019723,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2129559-7120416,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2129559-7265210,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2129559-803646,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2129559-922889,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2129559-94251
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Dec
|
pubmed:issn |
0305-1048
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pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
11
|
pubmed:volume |
18
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
7109-18
|
pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:2129559-Amino Acid Sequence,
pubmed-meshheading:2129559-Amino Acyl-tRNA Synthetases,
pubmed-meshheading:2129559-Aspartate-tRNA Ligase,
pubmed-meshheading:2129559-Base Sequence,
pubmed-meshheading:2129559-Cloning, Molecular,
pubmed-meshheading:2129559-Codon,
pubmed-meshheading:2129559-Escherichia coli,
pubmed-meshheading:2129559-Genes, Bacterial,
pubmed-meshheading:2129559-Lysine-tRNA Ligase,
pubmed-meshheading:2129559-Molecular Sequence Data,
pubmed-meshheading:2129559-Mutagenesis, Site-Directed,
pubmed-meshheading:2129559-Protein Biosynthesis,
pubmed-meshheading:2129559-RNA, Transfer, Amino Acyl,
pubmed-meshheading:2129559-Restriction Mapping,
pubmed-meshheading:2129559-Sequence Alignment,
pubmed-meshheading:2129559-Sequence Homology, Nucleic Acid
|
pubmed:year |
1990
|
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.
|
pubmed:affiliation |
Institut de Biologie Moléculaire et Cellulaire du CNRS, Strasbourg, France.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|