rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
7
|
pubmed:dateCreated |
1992-6-5
|
pubmed:abstractText |
Aminoacyl-tRNA synthetases interact with their cognate tRNAs in a highly specific fashion. We have examined the phenomenon that upon complex formation E. coli glutaminyl-tRNA synthetase destabilizes tRNA(Gln) causing chain scissions in the presence of Mg2+ ions. The phosphodiester bond cleavage produces 3'-phosphate and 5'-hydroxyl ends. This kind of experiment is useful for detecting conformational changes in tRNA. Our results show that the cleavage is synthetase-specific, that mutant and wild-type tRNA(Gln) species can assume a different conformation, and that modified nucleosides in tRNA enhance the structural stability of the molecule.
|
pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/1579445-1698276,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1579445-1718000,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1579445-1720569,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1579445-1857417,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1579445-1857423,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1579445-2047877,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1579445-2109304,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1579445-2174366,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1579445-2180700,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1579445-2187177,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1579445-220499,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1579445-2253707,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1579445-2330033,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1579445-2478363,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1579445-2479982,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1579445-2686030,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1579445-3054566,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1579445-3277187,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1579445-3304135,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1579445-3309332,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1579445-3331337,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1579445-343112,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1579445-3900415,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1579445-3911010,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1579445-6343077,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1579445-6343887,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1579445-6550536,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1579445-6559132,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1579445-781298
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Apr
|
pubmed:issn |
0305-1048
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
11
|
pubmed:volume |
20
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
1523-30
|
pubmed:dateRevised |
2009-11-18
|
pubmed:meshHeading |
pubmed-meshheading:1579445-Amino Acyl-tRNA Synthetases,
pubmed-meshheading:1579445-Base Sequence,
pubmed-meshheading:1579445-Escherichia coli,
pubmed-meshheading:1579445-Kinetics,
pubmed-meshheading:1579445-Magnesium,
pubmed-meshheading:1579445-Molecular Sequence Data,
pubmed-meshheading:1579445-Mutation,
pubmed-meshheading:1579445-Nucleic Acid Conformation,
pubmed-meshheading:1579445-RNA, Transfer, Gln,
pubmed-meshheading:1579445-RNA, Transfer, Trp
|
pubmed:year |
1992
|
pubmed:articleTitle |
Aminoacyl-tRNA synthetase-induced cleavage of tRNA.
|
pubmed:affiliation |
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06511.
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
|