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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
8
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pubmed:dateCreated |
1987-12-16
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pubmed:databankReference | |
pubmed:abstractText |
The ILS1 gene encoding for cytoplasmic isoleucyl-tRNA synthetase from Saccharomyces cerevisiae was subcloned from a 5.4-kb insert of the shuttle vector YEp13 to M13mp8 and M13mp9. Nucleotide sequence analysis of a 4.3-kb BamHI-HpaI fragment revealed a single open reading frame from which we deduced the amino-acid sequence of the enzyme. Independently obtained amino-acid sequence information from ten tryptic peptides of the purified enzyme confirmed the gene-derived structure. The enzyme is comprised of 1073 amino-acids consistent with earlier determinations of its molecular mass. The codon usage of ILS1 is typical of abundant yeast proteins. A significant homology to E. coli isoleucyl- and valyl-tRNA synthetases as well as to yeast valyl-tRNA synthetase was detected. The characteristic amino-acid residues of the aminoacyl-adenylate site and of the potential binding site of the 3'-end of tRNA found in other synthetases are present in the structure.
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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 |
Aug
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pubmed:issn |
0177-3593
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
368
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
971-9
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:3311074-Amino Acid Sequence,
pubmed-meshheading:3311074-Amino Acyl-tRNA Synthetases,
pubmed-meshheading:3311074-Base Sequence,
pubmed-meshheading:3311074-Computers,
pubmed-meshheading:3311074-DNA, Fungal,
pubmed-meshheading:3311074-Escherichia coli,
pubmed-meshheading:3311074-Isoleucine-tRNA Ligase,
pubmed-meshheading:3311074-Molecular Sequence Data,
pubmed-meshheading:3311074-Protein Biosynthesis,
pubmed-meshheading:3311074-Saccharomyces cerevisiae
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pubmed:year |
1987
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pubmed:articleTitle |
Structure of the yeast isoleucyl-tRNA synthetase gene (ILS1). DNA-sequence, amino-acid sequence of proteolytic peptides of the enzyme and comparison of the structure to those of other known aminoacyl-tRNA synthetases.
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pubmed:affiliation |
Abteilung Chemie des Max-Planck-Institutes für experimentelle Medizin, Göttingen.
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pubmed:publicationType |
Journal Article,
Comparative Study
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