2000
A Mutant Escherichia coli Tyrosyl-tRNA Synthetase Utilizes the Unnatural Amino Acid Azatyrosine More Efficiently than Tyrosine*
Hamano-Takaku F, Iwama T, Saito-Yano S, Takaku K, Monden Y, Kitabatake M, Söll D, Nishimura S. A Mutant Escherichia coli Tyrosyl-tRNA Synthetase Utilizes the Unnatural Amino Acid Azatyrosine More Efficiently than Tyrosine*. Journal Of Biological Chemistry 2000, 275: 40324-40328. PMID: 11006270, DOI: 10.1074/jbc.m003696200.Peer-Reviewed Original ResearchConceptsUnnatural amino acidsTyrosyl-tRNA synthetaseEscherichia coli tyrosyl-tRNA synthetasePosition 130Amino acidsVivo protein biosynthesisE. coli cellsAminoacyl-tRNA formationSingle point mutationTyrRS mutantsCellular proteinsProtein biosynthesisTYR geneMutant enzymesPlasmid libraryReplacement of phenylalanineColi cellsImmense potentialNormal phenotypeEfficient productionPoint mutationsTyrRSProteinPolymerase chain reaction techniqueSynthetase
1999
Cysteinyl‐tRNA formation: the last puzzle of aminoacyl‐tRNA synthesis
Li T, Graham D, Stathopoulos C, Haney P, Kim H, Vothknecht U, Kitabatake M, Hong K, Eggertsson G, Curnow A, Lin W, Celic I, Whitman W, Söll D. Cysteinyl‐tRNA formation: the last puzzle of aminoacyl‐tRNA synthesis. FEBS Letters 1999, 462: 302-306. PMID: 10622715, DOI: 10.1016/s0014-5793(99)01550-1.Peer-Reviewed Original ResearchConceptsLateral gene transferAminoacyl-tRNA synthesisCysteinyl-tRNA synthetaseEscherichia coli cysteinyl-tRNA synthetaseMolecular phylogenyPyrococcus sppMethanococcus jannaschiiMethanococcus maripaludisM. maripaludisMethanogenic archaeaMethanosarcina sppGene transferCysRSMethanosarcina barkeriGenesSpecific relativeLast puzzleSppOrthologsArchaeaPhylogenyJannaschiiMutantsLineagesOrganisms
1997
When protein engineering confronts the tRNA world
Schimmel P, Söll D. When protein engineering confronts the tRNA world. Proceedings Of The National Academy Of Sciences Of The United States Of America 1997, 94: 10007-10009. PMID: 9294151, PMCID: PMC33764, DOI: 10.1073/pnas.94.19.10007.Peer-Reviewed Original Research
1996
The C-terminal Extension of Yeast Seryl-tRNA Synthetase Affects Stability of the Enzyme and Its Substrate Affinity (*)
Weygand-Durasevic I, Lenhard B, Filipic S, Söll D. The C-terminal Extension of Yeast Seryl-tRNA Synthetase Affects Stability of the Enzyme and Its Substrate Affinity (*). Journal Of Biological Chemistry 1996, 271: 2455-2461. PMID: 8576207, DOI: 10.1074/jbc.271.5.2455.Peer-Reviewed Original Research
1992
Recognition of bases in Escherichia coli tRNA(Gln) by glutaminyl‐tRNA synthetase: a complete identity set.
Hayase Y, Jahn M, Rogers M, Sylvers L, Koizumi M, Inoue H, Ohtsuka E, Söll D. Recognition of bases in Escherichia coli tRNA(Gln) by glutaminyl‐tRNA synthetase: a complete identity set. The EMBO Journal 1992, 11: 4159-4165. PMID: 1396597, PMCID: PMC556926, DOI: 10.1002/j.1460-2075.1992.tb05509.x.Peer-Reviewed Original ResearchConceptsGlutaminyl-tRNA synthetaseRecognition of basesSet of tRNAsEscherichia coliCognate aminoacyl-tRNA synthetasesAminoacyl-tRNA synthetasesCorrect aminoacylationRecombinant RNA technologySet of nucleotidesNumber of mutantsGlutamine identityTRNA genesTRNA discriminationTransfer RNAExcellent systemGlnRFunctional importanceSingle deletionSpecific contactsRNA technologyBase changesSpecificity constantAminoacylationSpecific guanosineMutants