Lysyl-tRNA Synthetase of Bacillus stearothermophilus Molecular Cloning and Expression of the Gene

Bioscience, Biotechnology and Biochemistry

Volumn 64, Issue 2, 2000, Pages 432-437

  Takita, Teisuke ^a   Shimizu, Naofumi ^a   Sukata, Tokuo ^a   Hashimoto, Satoshi ^a   Akita, Eriko ^a   Yokota, Takuya ^a   Esaki, Nobuyoshi ^a   Soda, Kenji ^a   Inouye, Kuniyo ^a   Tonomura, Benichiro ^a,b  

^a KYOTO UNIVERSITY   (Japan)

^b KINKI UNIVERSITY   (Japan)

Author keywords

Bacillus stearothermophilus; Gene cloning; Gene expression; Lysyl tRNA synthetase

Indexed keywords

BACTERIAL DNA; LYSINE TRANSFER RNA LIGASE; RECOMBINANT PROTEIN;

AMINO ACID SEQUENCE; ARTICLE; CODON; ENZYMOLOGY; GENETICS; GEOBACILLUS STEAROTHERMOPHILUS; MOLECULAR GENETICS; NUCLEOTIDE SEQUENCE; SEQUENCE HOMOLOGY;

AMINO ACID SEQUENCE; BACILLUS STEAROTHERMOPHILUS; BASE SEQUENCE; CODON; DNA, BACTERIAL; LYSINE-TRNA LIGASE; MOLECULAR SEQUENCE DATA; RECOMBINANT PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID;

ESCHERICHIA COLI; GEOBACILLUS STEAROTHERMOPHILUS;

EID: 0034132313     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.64.432     Document Type: Article

References (23)

1. Arnez, J. G. and Moras, D., Structural and functional considerations of the aminoacylation reaction. Trends Biochem. Sci., 22, 159-164 (1997).
2. Eriani, G., Delarue, M., Poch, O., Gangloff, J., and Moras, D., Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs. Nature, 347, 203-206 (1990).
3. Takita, T., Ohkubo, Y., Shima, H., Muto, T., Shimizu, N., Sukata, T., Ito, H., Saito, Y., Inouye, K., Hiromi, K., and Tonomura, B., Lysyl-tRNA synthetase from Bacillus stearothermophilus. Purification, and fluorometric and kinetic analysis of the binding of substrates, L-lysine and ATP. J. Biochem., 119, 680-689 (1996) [Corrections: J. Biochem., 123, 1218 (1998)].
4. Takita, T., Hashimoto, S., Ohkubo, Y., Muto, T., Shimizu, N., Sukata, T., Inouye, K., Hiromi, K., and Tonomura, B., Lysyl-tRNA synthetase from Bacillus stearothermophilus. Formation and isolation of the enzyme Tysyladenylate complex and its analogue. J. Biochem., 121, 244-250 (1997).
5. Takita, T., Hashimoto, S., Inouye, K., and Tonomura, B., A new filter assay in the study of lysyl-tRNA synthetase from Bacillus stearothermophilus. Biosci. Biotechnol. Biochem., 61, 726-728 (1997).
6. Takita, T., Akita, E., Inouye, K., and Tonomura, B., Lysyl-tRNA synthetase from Bacillus stearothermophilus. Stopped-flow kinetic analysis of enzyme Tysyladenylate formation. J. Biochem., 124, 45-50 (1998).
7. Steers, E., Jr., Craven, G. R., Anfinsen, C. B., Bethune, J. L., Evidence for nonidentical chains in the /Tgalactosidase of Escherichia coli K12. J. Biol. Chem., 240, 2478-2484 (1965).
8. Tunasawa, S., Masaki, T., Hirose, M., Soejima, M., Sakiyama, F., Lysylendopeptidase. Tampakusitsu Kakusan Kouso (in Japanese), 31, 629-634 (1986).
9. Leveque, F., Plateau, P., Dessen, P., and Blanquet, S., Homology of lysS and lysU, the two Escherichia coli genes encoding distinct lysyl-tRNA synthetase species. Nucleic Acids Res., 18, 305-312 (1990).
10. Ausubel, F. M., Brent, R., Kingston, R. E., Moore, D. D., Seidman, J. G., Smith, J. A., and Struhl, K., Current protocols in molecular biology. 15.1. Enzymatic amplification of DNA by the polymerase chain reaction: Standard procedures and optimization. John Wiley & Sons, New York (1987).
11. Sanger, F., Nicklen, S., and Coulson, A. R., DNA sequencing with chain-terminating inhibitors. Proc. Natl. Acad. Sci. USA, 74, 5463-5467 (1977).
12. Clark, R. L. and Neidhardt, F. C., Roles of the two lysyl-tRNA synthetases of Escherichia coli: Analysis of nucleotide sequence and mutant behavior. J. Bac-teriol., 172, 3237-3243 (1990).
13. Mihalyi, E., Numerical values of the absorbances of the aromatic amino acids in acid, neutral, and alkaline solutions. J. Chem. Eng. Data, 13, 179-182 (1968).
14. Kunst, F., Ogasawara, N., Moszer, I., and 148 authors, The complete genome sequence of the Gram-positive bacterium Bacillus subtilis. Nature, 390, 249-256 (1997).
15. Ozkokmen, D., Birkelund, S., and Christiansen, G., Characterization of a Mycoplasma hominis gene encoding lysyl-tRNA synthetase (LysRS). FEMS Microbiology Letters, 116, 277-282 (1994).
16. Theiss, P., Karpas, A., and Wise, K. S., Antigenic topology of the P29 surface lipoprotein of Mycoplasma fermentans: differential display of epitopes results in high-frequency phase variation. Infect. Immun., 64, 1800-1809 (1996).
17. Chen, J., Brevet, A., Lapadat-Tapolsky, M., Blanquet, S., and Plateau, P., Properties of the lysyl-tRNA synthetase gene and product from the extreme thermophile Thermus thermophilus. J. Bac-teriol., 176, 2699-2705 (1994).
18. Chan, V. L. and Bingham, H. L., Lysyl-tRNA synthetase gene of Campylobacter jejuni. J. Bacteriol., 174, 695-701 (1992).
19. Mirande, M. and Waller, J. P., The yeast lysyl-tRNA synthetase gene. Evidence for general amino acid control of its expression and domain structure of the encoded protein. J. Biol. Chem., 263, 18443-18451 (1988).
20. Gatti, D. L. and Tzagoloff, A., Structure and evolution of a group of related aminoacyl-tRNA synthetases. J. Mol. Biol., 218, 557-568 (1991).
21. Ibba, M., Morgan, S., Curnow, A., Pridmore, D. R., Vothknecht, U. C., Gardner, W., Lin, W., Woese, C. R., and Soli, D., A euryarchaeal lysyl-tRNA synthetase: resemblance to class I synthetase. Science, 278, 1119-1122 (1997).
22. Onesti, S., Miller, A. D., and Brick, P., The crystal structure of the lysyl-tRNA synthetase (LysU) from Escherichia coli. Structure, 3, 163-176 (1995).
23. Cavarelli, J., Eriani, G., Rees, B., Rulf, M., Boeglin, M., Mitschler, A., Martin, F., Ganglolf, J., Thierry, J. C., and Moras, D., The active site of yeast aspar-tyl-tRNA synthetase: structural and functional aspects of the aminoacylation reaction. EMBO J., 13, 327-337 (1994).