This project aims at isolating mutant aminoacyl tRNA synthetases with altered recognition. The gene for Ala-tRNA synthetase has been cloned into two pBR322 recombinant plasmids. A plasmid carrying alaS is mutagenized in vitro and then transformed into an appropriate recipient. Selection is done for cells with a phenotype that could be due to the presence of a misrecognition mutant of Ala-tRNA synthetase. A number of mutants have been obtained. And an Ala-tRNA synthetase which recognizes tRNAI1e has been isolated. Various mutants that have already been isolated are to be characterized thoroughly and more mutants are to be prepared. These efforts should yield a variety of mutant Ala-tRNA synthetases having different specific tRNA recognition changes. Two plasmids carrying alaS have been partially mapped with restriction enzymes, and this analysis will continue. The alaS segment of one of these plasmids will be sequenced; from this, and from a limited amount of peptide sequencing, the entire amino acid sequence of the protein will be determined. The positional location of mutations that cause tRNA specificity changes will be identified. This information will enable us to test and to build upon existing ideas on how recognition is achieved and on the structural organization of tRNA binding regions.
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| Song, Youngzee; Zhou, Huihao; Vo, My-Nuong et al. (2017) Double mimicry evades tRNA synthetase editing by toxic vegetable-sourced non-proteinogenic amino acid. Nat Commun 8:2281 |
| Naganuma, Masahiro; Sekine, Shun-ichi; Chong, Yeeting Esther et al. (2014) The selective tRNA aminoacylation mechanism based on a single G•U pair. Nature 510:507-11 |
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| Klipcan, Liron; Safro, Mark; Schimmel, Paul (2013) Anticodon G recognition by tRNA synthetases mimics the tRNA core. Trends Biochem Sci 38:229-32 |
| Guo, Min; Schimmel, Paul (2013) Essential nontranslational functions of tRNA synthetases. Nat Chem Biol 9:145-53 |
| Zhou, Huihao; Sun, Litao; Yang, Xiang-Lei et al. (2013) ATP-directed capture of bioactive herbal-based medicine on human tRNA synthetase. Nature 494:121-4 |
| Park, Min Chul; Kang, Taehee; Jin, Da et al. (2012) Secreted human glycyl-tRNA synthetase implicated in defense against ERK-activated tumorigenesis. Proc Natl Acad Sci U S A 109:E640-7 |
| Guo, Min; Schimmel, Paul (2012) Structural analyses clarify the complex control of mistranslation by tRNA synthetases. Curr Opin Struct Biol 22:119-26 |
| Sajish, Mathew; Zhou, Quansheng; Kishi, Shuji et al. (2012) Trp-tRNA synthetase bridges DNA-PKcs to PARP-1 to link IFN-? and p53 signaling. Nat Chem Biol 8:547-54 |
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