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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
21
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pubmed:dateCreated |
1987-2-11
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pubmed:abstractText |
Conformations of tRNAfMet, free and methionyl-tRNA synthetase bound forms, are analyzed by using singlet-singlet energy transfer as a spectroscopic ruler. tRNAfMet(8-13,3'-Flc), tRNAfMet(8-13,D-Etd), and tRNAfMet(3'-Flc,D-Etd) are prepared by sequential chemical modifications. The methionyl-tRNA synthetase binding affinity of these double-labeled tRNAfMets is similar to those of unmodified tRNAfMet. The fluorescence properties of the individual fluorophore in these tRNAs, including emission spectra, anisotropy, and quenching by methionyl-tRNA synthetase, are similar to those of single-labeled tRNAfMet. The transfer efficiencies of double-labeled tRNAfMets, as determined by both donor quenching and sensitized emission, showed efficient energy transfer in all cases. Random orientation being assumed, the apparent distances are 25 A between 8-13 and D20, 44 A between 8-13 and the 3'-terminus, and 49 A between the 3'-terminus and D20, respectively, in free tRNAfMet. Upon binding of methionyl-tRNA synthetase, the apparent distances are 25 A between 8-13 and D20, 45 A between 8-13 and the 3'-terminus, and 54 A between the 3'-terminus and D20, respectively. These results provide topographic models of these specific locations in free and methionyl-tRNA synthetase bound tRNAfMet and suggest that the immobilized 3'-terminal arm in the amino acid acceptor stem bends toward the inner loop of the L-shaped tRNA upon binding of methionyl-tRNA synthetase.
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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/Amino Acyl-tRNA Synthetases,
http://linkedlifedata.com/resource/pubmed/chemical/Methionine-tRNA Ligase,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Transfer, Amino Acyl,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Transfer, Met,
http://linkedlifedata.com/resource/pubmed/chemical/tRNA, formylmethionine-
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0006-2960
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
21
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pubmed:volume |
25
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
6572-8
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:3641634-Amino Acyl-tRNA Synthetases,
pubmed-meshheading:3641634-Energy Transfer,
pubmed-meshheading:3641634-Kinetics,
pubmed-meshheading:3641634-Methionine-tRNA Ligase,
pubmed-meshheading:3641634-Nucleic Acid Conformation,
pubmed-meshheading:3641634-Protein Binding,
pubmed-meshheading:3641634-RNA, Transfer, Amino Acyl,
pubmed-meshheading:3641634-RNA, Transfer, Met,
pubmed-meshheading:3641634-Spectrometry, Fluorescence
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pubmed:year |
1986
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pubmed:articleTitle |
Topographic modeling of free and methionyl-tRNA synthetase bound tRNAfMet by singlet-singlet energy transfer: bending of the 3'-terminal arm in tRNAfMet.
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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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