Source:http://linkedlifedata.com/resource/pubmed/id/10471730
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
18
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pubmed:dateCreated |
1999-11-4
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pubmed:abstractText |
Sequence-specific interactions between aminoacyl-tRNA synthetases and their cognate tRNAs ensure both accurate RNA recognition and the efficient catalysis of aminoacylation. The effects of tRNA(Trp)variants on the aminoacylation reaction catalyzed by wild-type Escherichia coli tryptophanyl-tRNA synthe-tase (TrpRS) have now been investigated by stopped-flow fluorimetry, which allowed a pre-steady-state analysis to be undertaken. This showed that tRNA(Trp)identity has some effect on the ability of tRNA to bind the reaction intermediate TrpRS-tryptophanyl-adenylate, but predominantly affects the rate at which trypto-phan is transferred from TrpRS-tryptophanyl adenylate to tRNA. Use of the binding ( K (tRNA)) and rate constants ( k (4)) to determine the energetic levels of the various species in the aminoacylation reaction showed a difference of approximately 2 kcal mol(-1)in the barrier to transition state formation compared to wild-type for both tRNA(Trp)A-->C73 and. These results directly show that tRNA identity contributes to the degree of complementarity to the transition state for tRNA charging in the active site of an aminoacyl-tRNA synthetase:aminoacyl-adenylate:tRNA complex.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Monophosphate,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Transfer, Amino Acyl,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Transfer, Gln,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Transfer, Trp,
http://linkedlifedata.com/resource/pubmed/chemical/Tryptophan,
http://linkedlifedata.com/resource/pubmed/chemical/Tryptophan-tRNA Ligase,
http://linkedlifedata.com/resource/pubmed/chemical/tRNA, tryptophan-
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
1362-4962
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:day |
15
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pubmed:volume |
27
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3631-7
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pubmed:dateRevised |
2008-11-20
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pubmed:meshHeading |
pubmed-meshheading:10471730-Adenosine Monophosphate,
pubmed-meshheading:10471730-Base Sequence,
pubmed-meshheading:10471730-Binding Sites,
pubmed-meshheading:10471730-Catalysis,
pubmed-meshheading:10471730-Escherichia coli,
pubmed-meshheading:10471730-Fluorescence,
pubmed-meshheading:10471730-Kinetics,
pubmed-meshheading:10471730-Mutation,
pubmed-meshheading:10471730-Nucleic Acid Conformation,
pubmed-meshheading:10471730-RNA, Transfer, Amino Acyl,
pubmed-meshheading:10471730-RNA, Transfer, Gln,
pubmed-meshheading:10471730-RNA, Transfer, Trp,
pubmed-meshheading:10471730-Substrate Specificity,
pubmed-meshheading:10471730-Thermodynamics,
pubmed-meshheading:10471730-Tryptophan,
pubmed-meshheading:10471730-Tryptophan-tRNA Ligase
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pubmed:year |
1999
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pubmed:articleTitle |
Transfer RNA identity contributes to transition state stabilization during aminoacyl-tRNA synthesis.
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pubmed:affiliation |
Department of Molecular Biophysics and Biochemistry Yale University, New Haven, CT 06520-8114, USA. mibba@imbg.ku.dk
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.
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