Solvation change and ion release during aminoacylation by aminoacyl-tRNA synthetases
نویسندگان
چکیده
منابع مشابه
Aminoacyl-tRNA synthetases and aminoacylation of tRNA in the nucleus.
This review is focused on findings concerning the presence of translation apparatus components (aminoacyl-tRNA synthetases, aminoacyl-tRNA, elongation factors) as well as translation itself in the nucleus. A nuclear role of these molecules is unknown. New findings suggest that well-accepted model of spatial segregation of transcription and translation in eukaryotic cell may be oversimplifcation...
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Aminoacyl-tRNA synthetases (AARSs) are at the center of the question of the origin of life. They constitute a family of enzymes integrating the two levels of cellular organization: nucleic acids and proteins. AARSs arose early in evolution and are believed to be a group of ancient proteins. They are responsible for attaching amino acid residues to their cognate tRNA molecules, which is the firs...
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The accuracy of protein biosynthesis rests on the high fidelity with which aminoacyl-tRNA synthetases discriminate between tRNAs. Correct aminoacylation depends not only on identity elements (nucleotides in certain positions) in tRNA (1), but also on competition between different synthetases for a given tRNA (2). Here we describe in vivo and in vitro experiments which demonstrate how variations...
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In addition to their canonical roles in translation the aminoacyl-tRNA synthetases (ARSs) have developed secondary functions over the course of evolution. Many of these activities are associated with cellular survival and nutritional stress responses essential for homeostatic processes in higher eukaryotes. In particular, six ARSs and one associated factor have documented functions in angiogene...
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Previous proteomic analyses have shown that aminoacyl-tRNA synthetases (aaRSs) in many organisms can be modified by acetylation of lysine (Lys). In this present study, leucyl-tRNA synthetase and arginyl-tRNA synthetase from Escherichia coli (EcLeuRS and EcArgRS) were overexpressed and purified, and found to be acetylated on Lys residues by mass spectrometry (MS). Glutamine (Gln) scanning mutage...
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ژورنال
عنوان ژورنال: Nucleic Acids Research
سال: 2003
ISSN: 1362-4962
DOI: 10.1093/nar/gkg779