ПЛР-ампліфікація, клонування та секвенування фрагмента кДНК, що кодує нуклеотидзв'язуючий домен тирозил-тРНК синтетази ссавців
DOI:
https://doi.org/10.7124/bc.00044BАнотація
Проведено ПЛР-ампліфікацію, клонування та секвенування кДНК-фрагмента, шо кодує N-кінцевий нуклеотидзв'язуючий домен (згортку Россмана) тирозил-тРНК синтетази ссавців. Вперше виявлено унікальний варіант консервативного HIGH-подібного мотиву, HVAY, у якому залишок гліцину, що раніше вважався абсолютно консервативним для всіх АРСаз І структурного класу, замінений на залишок аланіну.Посилання
Kisselev LL, Favorova OO, Lavrik OI. Biosynthesis of proteins from amino acids to aminoacyl-tRNA. Moscow, Nauka, 1984; 408 p.
Schimmel P. Classes of aminoacyl-tRNA synthetases and the establishment of the genetic code. Trends Biochem Sci. 1991;16(1):1-3. Review.
Moras D. Aminoacyl-tRNA synthetases. Curr Biol. 1992; 2: 138-42.
Rossmann MG, Moras D, Olsen KW. Chemical and biological evolution of nucleotide-binding protein. Nature. 1974;250(463):194-9.
Bhat TN, Blow DM, Brick P, Nyborg J. Tyrosyl-tRNA synthetase forms a mononucleotide-binding fold. J Mol Biol. 1982;158(4):699-709.
Eriani G, Delarue M, Poch O, Gangloff J, Moras D. Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs. Nature. 1990;347(6289):203-6.
Cusack S, Berthet-Colominas C, H?rtlein M, Nassar N, Leberman R. A second class of synthetase structure revealed by X-ray analysis of Escherichia coli seryl-tRNA synthetase at 2.5 A. Nature. 1990;347(6290):249-55.
Mirande M. Aminoacyl-tRNA synthetase family from prokaryotes and eukaryotes: structural domains and their implications. Prog Nucleic Acid Res Mol Biol. 1991;40:95-142.
Korneliuk AI, Kurochkin IV, Matsuka GKh. Tyrosyl-tRNA synthetase from the bovine liver. Isolation and physico-chemical properties. Mol Biol (Mosk). 1988;22(1):176-86.
Ribkinska TA, Vartanyan OA, Filonenko VV, Sidorik LL, Kornelyuk AI, Beresten SF. A method for selection of hybridomas, secreting monoclonal antibodies against tyrosyl-tRNA synthetase, based on monitoring of the enzymatic activity. Biopolym Cell. 1990; 6(4):97-101
Ribkinska TA, Kornelyuk AI, Beresten SF, Matsuka GKh. The immunochemical approach for studies of structure tyrosyl-tRNA synthetase from bovine liver. Biopolym Cell. 1991; 7(5):33-6.
Gnatenko DV, Korneliuk AI, Matsuka GKh. Tyrosyl-tRNA-synthetase from bovine liver. Functional role of histidine residues. Bioorg Khim. 1991;17(8):1033-7.
Gnatenko DV, Korneliuk AI, Lavrik OI. Chemical modification of lysine residues in tyrosyl-tRNA-synthetase from cattle liver using pyridoxal-5'-phosphate. Biokhimiia. 1991;56(11):1984-90.
Nishimura A, Morita M, Nishimura Y, Sugino Y. A rapid and highly efficient method for preparation of competent Escherichia coli cells. Nucleic Acids Res. 1990;18(20):6169.
Birnboim HC, Doly J. A rapid alkaline extraction procedure for screening recombinant plasmid DNA. Nucleic Acids Res. 1979;7(6):1513-23.
Chow CM, RajBhandary UL. Saccharomyces cerevisiae cytoplasmic tyrosyl-tRNA synthetase gene. Isolation by complementation of a mutant Escherichia coli suppressor tRNA defective in aminoacylation and sequence analysis. J Biol Chem. 1993;268(17):12855-63.
Barker DG, Bruton CJ, Winter G. The tyrosyl-tRNA synthetase from Escherichia coli. Complete nucleotide sequence of the structural gene. FEBS Lett. 1982;150(2):419-23.
Winter G, Koch GL, Hartley BS, Barker DG. The amino acid sequence of the tyrosyl-tRNA synthetase from Bacillus stearothermophilus. Eur J Biochem. 1983;132(2):383-7.
Brick P, Bhat TN, Blow DM. Structure of tyrosyl-tRNA synthetase refined at 2.3 A resolution. Interaction of the enzyme with the tyrosyl adenylate intermediate. J Mol Biol. 1989;208(1):83-98.
