Linked Life Data

2467006

Source:http://linkedlifedata.com/resource/pubmed/id/2467006

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1989-5-2
pubmed:abstractText
The aminoacylation of transfer RNA is a key step of translation since it relates amino acids to anticodons. To understand how the tyrosyl-tRNA synthetase (TyrTS) from Bacillus stearothermophilus recognizes tRNA(Tyr), we constructed 14 new mutant TyrTS by site-directed mutagenesis, determined their kinetic properties and used these and previous data to construct a detailed structural model of the complex between TyrTS and the acceptor arm of tRNA(Tyr). In the model Arg207, Lys208, Asn 146 and Glu 152 interact with phosphate groups. A contact between guanine 1 and Trp 196 is unspecific. Adenine 73, the fourth base from the 3' end, is specifically recognized through Trp 196 and the main-chain carbonyl of Ala150. At the active site, adenine 76 might interact with Lys82 and Arg86. There is a tight complementarity in shape between the tRNA and the synthetase. TyrTS and tRNA(Tyr) form an additional contact, in the vicinity of adenine 73, when their complex goes from the initial state to the transition state. The rate of aminoacylation, through the precise recognition of adenine 73, could thus be an important factor of discrimination by TyrTS among tRNAs.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0022-2836
pubmed:author
pubmed:issnType
Print
pubmed:day
20
pubmed:volume
205
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
729-35
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
Structural and kinetic bases for the recognition of tRNATyr by tyrosyl-tRNA synthetase.
pubmed:affiliation
Unité de Biochimie des Régulations Cellulaires (C N RS U RA D1129), Institut Pasteur, Paris, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't