Threonyl-tRNA synthetase from Chinese hamster ovary cells is phosphorylated on serine.
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چکیده
منابع مشابه
Increased levels of threonyl-tRNA synthetase in a borrelidin-resistant Chinese hamster ovary cell line.
The growth of Chinese hamster ovary cells in medium containing reduced concentrations of threonine is inhibited by borrelidin, a macrolide antibiotic. Borrelidin-resistant clones have been isolated after ethyl methanesulfonate mutagenesis. One clone, 1C-1, has a 3-fold increased level of threonyl-tRNA synthetase [L-threonine:tRNAThr ligase (AMP-forming), EC 6.1.1.3] as determined by both activi...
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The growth inhibitory activity of tiazofurin toward adenosine kinase deficient Chinese hamster ovary (CHO) cells was partially reversed by the presence of nicotinamide riboside. Similarly, the formation of tiazofurin 5'-monophosphate and the active metabolite, tiazofurin 5'-adenine dinucleotide could be partially inhibited by 100 microM nicotinamide riboside in CHO cells and substantially inhib...
متن کاملIdentification of borrelidin binding site on threonyl-tRNA synthetase.
Borrelidin exhibits a wide spectrum of biological activities and has been considered as a non-competitive inhibitor of threonyl-tRNA synthetase (ThrRS). However, the detailed mechanisms of borrelidin against ThrRS, especially borrelidin binding site on ThrRS, are still unclear, which limits the development of novel borrelidin derivatives and rational design of structure-based ThrRS inhibitors. ...
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Proteinase 3(PR3) is a human polymorphonuclear leukocyte serine proteinase and is the main target antigen for antineutrophil cytoplasmic antibodies (ANCA) found in Wegener's granulomatosis (WG). We developed a stable expression system for conformationally intact recombinant PR3 (rPR3) in Chinese hamster ovary cells (CHO-cells). The part of PR3 cDNA that encoded the active form of PR3 was s...
متن کاملEVOLUTION AND tRNA RECOGNITION OF THREONYL-tRNA SYNTHETASE FROM AN EXTREME THERMOPHILIC ARCHAEON, Aeropyrum pernix K1
An extreme thermophilic archaeon, Aeropyrum pernix K1 possesses two possible threonyl-tRNA synthetase genes. Sequence homology analysis of these genes with other species threonyl-tRNA synthetase showed that the shorter gene did not possess motif-2 and motif-3 of catalytic core that were conserved in class II aminoacyl-tRNA synthetases. On the other hand, the longer gene had almost all amino aci...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1984
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)90837-9