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Homologous Trans ‐editing Factors with Broad Substrate Specificity Prevent Global Mistranslation
Author(s) -
MusierForsyth Karin,
Bacusmo Jo Marie,
Bakhtina Marina,
Cantara William A.,
Goto Yuki,
Kuzmishin Alexandra B.,
Suga Hiroaki
Publication year - 2019
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.2019.33.1_supplement.91.2
Subject(s) - transfer rna , amino acyl trna synthetases , amino acid , translation (biology) , genetic code , aminoacyl trna synthetase , aminoacylation , biology , proofreading , genome editing , computational biology , protein biosynthesis , rna editing , genetics , biochemistry , gene , rna , genome , messenger rna , polymerase
Accurate translation of genetic information is determined, in part, by aminoacyl‐tRNA synthetases (ARSs), which are responsible for the correct pairing of amino acids with their cognate tRNA adaptors. However, these reactions are susceptible to errors due to structural similarities of amino acids that challenge the specificity of some synthetases and promote the incorporation of amino acids at wrong codons during protein synthesis (mistranslation). To maintain translational fidelity, many synthetases have expanded their aminoacylation capabilities to include editing mechanisms that involve deacylation of the mischarged tRNA (“post‐transfer editing”) in a second catalytic site. In addition, single‐domain homologs of some ARS editing domains catalyze post‐transfer editing in trans . A global bioinformatics analysis has uncovered distinct trans ‐editing domains related to the bacterial prolyl‐tRNA synthetase (ProRS) post‐transfer editing domain, which is known to clear Ala‐tRNA Pro . While a subset of these trans‐ editing proteins correct ProRS‐dependent errors Ala‐ and Cys‐tRNA Pro recent studies have revealed surprising substrate specificities that include non‐proteinogenic amino acids. In addition, whereas some editing domains have borrowed some aspects of tRNA recognition from the parent aminoacyl‐tRNA synthetase, semi‐promiscuous editing may offer advantages to cells. This abstract is from the Experimental Biology 2019 Meeting. There is no full text article associated with this abstract published in The FASEB Journal .