rdf:type |
|
lifeskim:mentions |
umls-concept:C0035711,
umls-concept:C0035731,
umls-concept:C0036843,
umls-concept:C0077366,
umls-concept:C0086418,
umls-concept:C0205372,
umls-concept:C0547040,
umls-concept:C0678594,
umls-concept:C1421182,
umls-concept:C1514562,
umls-concept:C1537998,
umls-concept:C1710236,
umls-concept:C1880177,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221
|
pubmed:issue |
3
|
pubmed:dateCreated |
1998-7-6
|
pubmed:abstractText |
The recognition process of tRNA(Ser) and tRNA(Sec) by human seryl-tRNA synthetase (SerRS) was studied using T7 transcripts representing defined regions of human tRNA(Ser) or tRNA(Sec) and the influence of the tRNA elements on serylation and tertiary structure was elucidated. The anticodon arms of both tRNAs showed no contribution to serylation in contrast to the acceptor stems and the long extra arms. D and T arms were only involved in formation of the L-shaped tRNA structure, not in the recognition process between tRNAs and SerRS. This is the first report of microhelices adapted from human tRNAs being aminoacylated by their homologous synthetase.
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Anticodon,
http://linkedlifedata.com/resource/pubmed/chemical/RNA,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Transfer, Amino Acid-Specific,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Transfer, Ser,
http://linkedlifedata.com/resource/pubmed/chemical/Serine,
http://linkedlifedata.com/resource/pubmed/chemical/Serine-tRNA Ligase,
http://linkedlifedata.com/resource/pubmed/chemical/tRNA, selenocysteine-
|
pubmed:status |
MEDLINE
|
pubmed:month |
May
|
pubmed:issn |
0014-5793
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
15
|
pubmed:volume |
427
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
315-9
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading |
pubmed-meshheading:9637248-Anticodon,
pubmed-meshheading:9637248-HeLa Cells,
pubmed-meshheading:9637248-Humans,
pubmed-meshheading:9637248-Kinetics,
pubmed-meshheading:9637248-Mutation,
pubmed-meshheading:9637248-Nucleic Acid Conformation,
pubmed-meshheading:9637248-Protein Structure, Tertiary,
pubmed-meshheading:9637248-RNA,
pubmed-meshheading:9637248-RNA, Transfer, Amino Acid-Specific,
pubmed-meshheading:9637248-RNA, Transfer, Ser,
pubmed-meshheading:9637248-Serine,
pubmed-meshheading:9637248-Serine-tRNA Ligase
|
pubmed:year |
1998
|
pubmed:articleTitle |
Minimal tRNA(Ser) and tRNA(Sec) substrates for human seryl-tRNA synthetase: contribution of tRNA domains to serylation and tertiary structure.
|
pubmed:affiliation |
Institut für Biochemie, Bayerische Julius-Maximilians-Universität, Biozentrum, Würzburg, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|