Crucial Role of the HIGH-loop Lysine for the Catalytic Activity of Arginyl-tRNA Synthetase

Journal of Biological Chemistry

Volumn 276, Issue 6, 2001, Pages 3723-3726

  Sekine, Shun Ichi ^a   Shimada, Atsushi ^b   Nureki, Osamu ^b   Cavarelli, Jean ^c   Moras, Dino ^c   Vassylyev, Dmitry G ^a   Yokoyama, Shigeyuki ^a,b  

^a RIKEN HARIMA INSTITUTE   (Japan)

^b UNIVERSITY OF TOKYO   (Japan)

^c INSTITUT DE GÉNÉTIQUE ET DE BIOLOGIE MOLÉCULAIRE ET CELLULAIRE   (France)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CATALYSIS; MUTAGENESIS; RNA; STABILIZATION;

SEQUENCE ANALYSIS;

ENZYMES;

ARGININE TRANSFER RNA LIGASE; GLYCINE; HISTIDINE; ISOLEUCINE; LYSINE; PROTEIN SUBUNIT; PSEUDOMONIC ACID;

ARTICLE; CONTROLLED STUDY; DRUG DESIGN; DRUG TARGETING; ENZYME ACTIVE SITE; ENZYME ACTIVITY; NONHUMAN; PRIORITY JOURNAL; PROTEIN MOTIF; REACTION ANALYSIS; RNA TRANSLATION; SACCHAROMYCES CEREVISIAE; SEQUENCE ANALYSIS; SITE DIRECTED MUTAGENESIS; THERMUS THERMOPHILUS; AMINO ACID SEQUENCE; CATALYSIS; CHEMICAL STRUCTURE; CHEMISTRY; METABOLISM; MOLECULAR GENETICS; PROTEIN CONFORMATION; SEQUENCE HOMOLOGY;

NEGIBACTERIA; SACCHAROMYCES; SACCHAROMYCES CEREVISIAE; THERMUS; THERMUS THERMOPHILUS;

AMINO ACID SEQUENCE; ARGININE-TRNA LIGASE; CATALYSIS; LYSINE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION; SEQUENCE HOMOLOGY, AMINO ACID;

EID: 0035830940     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.C000756200     Document Type: Article

References (21)

1. Eriani, G., Delarue, M., Poch, O., Gangloff, J., and Moras, D. (1990) Nature 347, 203-206
2. Cusack, S. (1995) Nat. Struct. Biol. 2, 824-831
3. Fersht, A. R., Knill-Jones, J. W., Bedouelle, H., and Winter, G. (1988) Biochemistry 27, 1581-1587
4. Mechulam, Y., Dardel, F., Le Corre, D., Blanquet, S., and Fayat, G. (1991) J. Mol. Biol. 217, 465-475
5. Schmitt, E., Meinnel, T., Blanquet, S., and Mechulam, Y. (1994) J. Mol. Biol. 242, 566-576
6. Meinnel, T., Mechulam, Y., and Blanquet, S. (1995) in tRNA. Structure, Biosynthesis, and Function (Söll, D., and RajBhandary, U. L., eds) pp. 251-292, ASM Press, Washington, D. C.
7. Rould, M. A., Perona, J. J., Söll, D., and Steitz, T. A. (1989) Science 246, 1135-1142
8. Doublié, S., Bricogne, G., Gilmore, C., and Carter, C. W., Jr. (1995) Structure (Lond.) 3, 17-31
9. Rath, V. L., Silvian, L. F., Beijer, B., Sproat, B. S., and Steitz, T. A. (1998) Structure (Lond.) 6, 439-449
10. Perona, J. J., Rould, M. A., and Steitz, T. A. (1993) Biochemistry 32, 8758-8771
11. Cavarelli, J., Delagoutte, B., Eriani, G., Gangloff, J., and Moras, D. (1998) EMBO J. 17, 5438-5448
12. Zawadzki, V., and Gross, H. J. (1991) Nucleic Acids Res. 19, 1948
13. Nureki, O., Niimi, T., Muramatsu, T., Kanno, H., Kohno, T., Florentz, C., Giegé, R., and Yokoyama, S. (1994) J. Mol. Biol. 236, 710-724
14. Sekine, S., Nureki, O., Sakamoto, K., Niimi, T., Tateno, M., Go, M., Kohno, T., Brisson, A., Lapointe, J., and Yokoyama, S. (1996) J. Mol. Biol. 256, 685-700
15. Calendar, R., and Berg, P. (1966) Biochemistry 5, 1681-1690
16. Mitra, K., and Mehler, A. H. (1966) J. Biol. Chem. 241, 5161-5162
17. Mitra, S. K., and Mehler, A. H. (1967) J. Biol. Chem. 242, 5490-5494
18. Mehler, A. H., and Mitra, K. (1966) J. Biol. Chem. 242, 5495-5499
19. Schimmel, P., Tao, J., and Hill, J. (1998) FASEB J. 12, 1599-1609
20. Kraulis, P. J. (1991) J. Appl. Crystallogr. 24, 946-950
21. Merritt, E. A., and Murphy, M. E. P. (1994) Acta Crystallogr. Sect. D Biol. Crystallogr. 50, 869-873