rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5452
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pubmed:dateCreated |
2000-2-7
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pubmed:abstractText |
The genome sequences of certain archaea do not contain recognizable cysteinyl-transfer RNA (tRNA) synthetases, which are essential for messenger RNA-encoded protein synthesis. However, a single cysteinyl-tRNA synthetase activity was detected and purified from one such organism, Methanococcus jannaschii. The amino-terminal sequence of this protein corresponded to the predicted sequence of prolyl-tRNA synthetase. Biochemical and genetic analyses indicated that this archaeal form of prolyl-tRNA synthetase can synthesize both cysteinyl-tRNA(Cys) and prolyl-tRNA(Pro). The ability of one enzyme to provide two aminoacyl-tRNAs for protein synthesis raises questions about concepts of substrate specificity in protein synthesis and may provide insights into the evolutionary origins of this process.
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pubmed:commentsCorrections |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Amino Acyl-tRNA Synthetases,
http://linkedlifedata.com/resource/pubmed/chemical/Cysteine,
http://linkedlifedata.com/resource/pubmed/chemical/Multienzyme Complexes,
http://linkedlifedata.com/resource/pubmed/chemical/Proline,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Transfer, Amino Acyl,
http://linkedlifedata.com/resource/pubmed/chemical/cysteinyl-tRNA synthetase,
http://linkedlifedata.com/resource/pubmed/chemical/prolyl T RNA synthetase,
http://linkedlifedata.com/resource/pubmed/chemical/tRNA, cysteine-,
http://linkedlifedata.com/resource/pubmed/chemical/tRNA, proline-
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0036-8075
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
21
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pubmed:volume |
287
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
479-82
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pubmed:dateRevised |
2007-3-19
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pubmed:meshHeading |
pubmed-meshheading:10642548-Amino Acyl-tRNA Synthetases,
pubmed-meshheading:10642548-Binding Sites,
pubmed-meshheading:10642548-Cysteine,
pubmed-meshheading:10642548-Escherichia coli,
pubmed-meshheading:10642548-Evolution, Molecular,
pubmed-meshheading:10642548-Genes, Archaeal,
pubmed-meshheading:10642548-Methanococcus,
pubmed-meshheading:10642548-Multienzyme Complexes,
pubmed-meshheading:10642548-Proline,
pubmed-meshheading:10642548-RNA, Transfer, Amino Acyl,
pubmed-meshheading:10642548-Sequence Analysis, Protein,
pubmed-meshheading:10642548-Substrate Specificity,
pubmed-meshheading:10642548-Transfer RNA Aminoacylation,
pubmed-meshheading:10642548-Transformation, Bacterial
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pubmed:year |
2000
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pubmed:articleTitle |
One polypeptide with two aminoacyl-tRNA synthetase activities.
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pubmed:affiliation |
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520-8114, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.
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