FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2000930522> ?p ?o ?g. }

• W2000930522 endingPage "914" @default.
• W2000930522 startingPage "907" @default.
• W2000930522 abstract "In this review, I have brought together and compared the available data on the interaction between tRNATyr and tyrosyl-tRNA synthetases (TyrTS) of prokaryotic origins. The amino acid sequences of the heterologous TyrTS that can charge Escherichia coli tRNATyr, show that the residues involved in the binding and recognition of tyrosine are strictly conserved whereas those involved in the interaction with tRNATyr are only weakly similar. The results of in vivo genetic complementation experiments indicate that the identity elements of tRNAs and the recognition mechanisms of such elements by the synthetases have been conserved during evolution. Heterologous or mutant tRNATyr are quantitatively charged by E coli TyrTS; the set of their common residues contains less than 10 elements if one excludes the invariant and semi-invariant residues of tRNAs. The residues of this set are candidates for a specific recognition by TyrTS. So far, adenosine-73 is the only residue for which a specific recognition of the base has been demonstrated. The residues that might serve as identify elements for E coli tRNATyr [McClain WH, Nicholas Jr HB (1987) J Mol Biol 194, 635–642] do not belong to the above set of conserved residues and therefore probably play negative roles, enabling tRNATyr to avoid non-cognate synthetases. Comparison of the charging and stability properties of mutant tRNATyrsu+3 shows that bases 1 and 72 must pair (either by Watson-Crick or non-canonical hydrogen bonds) and adopt a geometry which is compatible with the helical structure of the acceptor stem in order for the mutant tRNATyr to be charged with tyrosine. If bases 1 and 72 or bases 2 and 71 cannot form such pairings, the suppressor phenotype of the mutant tRNATyrsu+3 becomes thermosensitive. The weakening of base pair 1 / 72 by mutation or the change of adenosine-73 into guanosine results in the charging of tRNATyrsu+3 with glutamine. Comparison of the structural model of the TyrTS/tRNATyr complex with the crystallographic structure of the GlnTS/tRNAGln complex indicates that the mechanisms for the recognition of the acceptor arm are different in the 2 cases. Chemical attack and molecular modeling experiments have indicated that the acceptor end of tRNATyr … CCA3′-OH, remains mobile after the initial binding of tRNATyr to TyrTS." @default.
• W2000930522 created "2016-06-24" @default.
• W2000930522 creator A5064506883 @default.
• W2000930522 creator A5076354181 @default.
• W2000930522 date "1970-03-01" @default.
• W2000930522 modified "2023-10-12" @default.
• W2000930522 title "E. coli tyrosine transfer RNA: Chemical modification of thiouridine to uridine" @default.
• W2000930522 cites W1556273208 @default.
• W2000930522 cites W1988163980 @default.
• W2000930522 cites W1996179635 @default.
• W2000930522 cites W2000146904 @default.
• W2000930522 cites W2000973771 @default.
• W2000930522 cites W2017640834 @default.
• W2000930522 cites W2071371565 @default.
• W2000930522 cites W2077720714 @default.
• W2000930522 cites W2091474276 @default.
• W2000930522 cites W2131783246 @default.
• W2000930522 cites W7875858 @default.
• W2000930522 doi "https://doi.org/10.1016/0006-291x(70)90807-7" @default.
• W2000930522 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/4908539" @default.
• W2000930522 hasPublicationYear "1970" @default.
• W2000930522 type Work @default.
• W2000930522 sameAs 2000930522 @default.
• W2000930522 citedByCount "25" @default.
• W2000930522 crossrefType "journal-article" @default.
• W2000930522 hasAuthorship W2000930522A5064506883 @default.
• W2000930522 hasAuthorship W2000930522A5076354181 @default.
• W2000930522 hasConcept C104317684 @default.
• W2000930522 hasConcept C143065580 @default.
• W2000930522 hasConcept C153957851 @default.
• W2000930522 hasConcept C185581394 @default.
• W2000930522 hasConcept C185592680 @default.
• W2000930522 hasConcept C188082640 @default.
• W2000930522 hasConcept C2776165026 @default.
• W2000930522 hasConcept C54355233 @default.
• W2000930522 hasConcept C547475151 @default.
• W2000930522 hasConcept C552990157 @default.
• W2000930522 hasConcept C55493867 @default.
• W2000930522 hasConcept C67705224 @default.
• W2000930522 hasConcept C71240020 @default.
• W2000930522 hasConcept C86803240 @default.
• W2000930522 hasConceptScore W2000930522C104317684 @default.
• W2000930522 hasConceptScore W2000930522C143065580 @default.
• W2000930522 hasConceptScore W2000930522C153957851 @default.
• W2000930522 hasConceptScore W2000930522C185581394 @default.
• W2000930522 hasConceptScore W2000930522C185592680 @default.
• W2000930522 hasConceptScore W2000930522C188082640 @default.
• W2000930522 hasConceptScore W2000930522C2776165026 @default.
• W2000930522 hasConceptScore W2000930522C54355233 @default.
• W2000930522 hasConceptScore W2000930522C547475151 @default.
• W2000930522 hasConceptScore W2000930522C552990157 @default.
• W2000930522 hasConceptScore W2000930522C55493867 @default.
• W2000930522 hasConceptScore W2000930522C67705224 @default.
• W2000930522 hasConceptScore W2000930522C71240020 @default.
• W2000930522 hasConceptScore W2000930522C86803240 @default.
• W2000930522 hasIssue "5" @default.
• W2000930522 hasLocation W20009305221 @default.
• W2000930522 hasLocation W20009305222 @default.
• W2000930522 hasOpenAccess W2000930522 @default.
• W2000930522 hasPrimaryLocation W20009305221 @default.
• W2000930522 hasRelatedWork W1500684591 @default.
• W2000930522 hasRelatedWork W1518010816 @default.
• W2000930522 hasRelatedWork W1587647201 @default.
• W2000930522 hasRelatedWork W1976496938 @default.
• W2000930522 hasRelatedWork W1988188960 @default.
• W2000930522 hasRelatedWork W2036810953 @default.
• W2000930522 hasRelatedWork W2086019465 @default.
• W2000930522 hasRelatedWork W2128292801 @default.
• W2000930522 hasRelatedWork W2154338693 @default.
• W2000930522 hasRelatedWork W2189178478 @default.
• W2000930522 hasVolume "38" @default.
• W2000930522 isParatext "false" @default.
• W2000930522 isRetracted "false" @default.
• W2000930522 magId "2000930522" @default.
• W2000930522 workType "article" @default.