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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
1993-8-5
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pubmed:databankReference | |
pubmed:abstractText |
The genes of aspartyl-tRNA synthetase (AspRS) from two Thermus thermophilus strain VK-1 and HB8, have been cloned and sequenced. Their nucleotidic sequences code for the same protein which displays the three characteristic motifs of class II aminoacyl-tRNA synthetases. This enzyme shows 50% identity with Escherichia coli AspRS, over the totality of the chain (580 amino acids). A comparison with the eukaryotic yeast cytoplasmic AspRS indicates the presence in the prokaryotic AspRS of an extra domain between motifs 2 and 3 much larger than in the eukaryotic ones. When its gene is under the control of the tac promoter of the expression vector pKK223-3, the protein is efficiently overexpressed as a thermostable protein in E. coli. It can be further purified to homogeneity using a heat treatment followed by a single anion exchange chromatography. Single crystals of the pure protein, diffracting at least to 2.2 A resolution (space group P2(1)2(1)2(1), a = 61.4 A, b = 156.1 A, c = 177.3 A) are routinely obtained. The same crystals have previously been described as crystals of threonyl-tRNA synthetase [1].
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0014-5793
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
5
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pubmed:volume |
325
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pubmed:geneSymbol |
aspS
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
183-6
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:8319804-Amino Acid Sequence,
pubmed-meshheading:8319804-Aspartate-tRNA Ligase,
pubmed-meshheading:8319804-Base Sequence,
pubmed-meshheading:8319804-Cloning, Molecular,
pubmed-meshheading:8319804-Crystallization,
pubmed-meshheading:8319804-Genes, Bacterial,
pubmed-meshheading:8319804-Models, Molecular,
pubmed-meshheading:8319804-Molecular Sequence Data,
pubmed-meshheading:8319804-Oligodeoxyribonucleotides,
pubmed-meshheading:8319804-Sequence Homology, Amino Acid,
pubmed-meshheading:8319804-Thermus thermophilus
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pubmed:year |
1993
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pubmed:articleTitle |
Sequence, overproduction and crystallization of aspartyl-tRNA synthetase from Thermus thermophilus. Implications for the structure of prokaryotic aspartyl-tRNA synthetases.
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pubmed:affiliation |
Laboratoire de Biochimie, URA 240 CNRS, Ecole Polytechnique, Palaiseau, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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