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Functional expansion of human tRNA synthetases achieved by structural inventions
Author(s) -
Guo Min,
Schimmel Paul,
Yang Xiang-Lei
Publication year - 2010
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2009.11.064
Subject(s) - transfer rna , aminoacylation , aminoacyl trna synthetase , amino acid , biology , protein biosynthesis , translation (biology) , amino acyl trna synthetases , genetic code , functional diversity , biochemistry , genetics , computational biology , rna , gene , messenger rna , ecology
Known as an essential component of the translational apparatus, the aminoacyl‐tRNA synthetase family catalyzes the first step reaction in protein synthesis, that is, to specifically attach each amino acid to its cognate tRNA. While preserving this essential role, tRNA synthetases developed other roles during evolution. Human tRNA synthetases, in particular, have diverse functions in different pathways involving angiogenesis, inflammation and apoptosis. The functional diversity is further illustrated in the association with various diseases through genetic mutations that do not affect aminoacylation or protein synthesis. Here we review the accumulated knowledge on how human tRNA synthetases used structural inventions to achieve functional expansions.