Expression and efficient export of enzymatically active Mycobacterium tuberculosis glutamine synthetase in Mycobacterium smegmatis and evidence that the information for export is contained within the protein

Journal of Biological Chemistry

Volumn 272, Issue 36, 1997, Pages 22728-22735

  Harth, Günter ^a   Horwitz, Marcus A ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

GLUTAMATE AMMONIA LIGASE; NITROGEN;

AMINO TERMINAL SEQUENCE; ARTICLE; ENZYME RELEASE; ESCHERICHIA COLI; GENETIC COMPLEMENTATION; MOLECULAR WEIGHT; MYCOBACTERIUM SMEGMATIS; MYCOBACTERIUM TUBERCULOSIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN TRANSPORT;

AMINO ACID SEQUENCE; BASE SEQUENCE; CLONING, MOLECULAR; DNA, BACTERIAL; GLUTAMATE-AMMONIA LIGASE; MOLECULAR SEQUENCE DATA; MYCOBACTERIUM; MYCOBACTERIUM TUBERCULOSIS; RECOMBINANT PROTEINS; TRANSCRIPTION, GENETIC;

BACTERIA (MICROORGANISMS); ESCHERICHIA; ESCHERICHIA COLI; MYCOBACTERIUM SMEGMATIS; MYCOBACTERIUM TUBERCULOSIS;

EID: 0030928121     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.272.36.22728     Document Type: Article

References (21)

1. Kochi, A. (1991) Tubercle 72, 1-6
2. Centers for Disease Control (1991) MMWR Morb. Mortal. Wkly. Rep. 40, 585-591
3. Harth, G., Clemens, D. L., and Horwitz, M. A. (1994) Proc. Natl. Acad. Sci. U. S. A. 91, 9342-9346
4. Garbe, T. R., Barathi, J., Barnini, S., Zhang, Y., Abou-Zeid, C., Tang, D., Mukherjee, R., and Young, D. B. (1994) Microbiology 140, 133-138
5. Hanahan, D. (1983) J. Mol. Biol. 166, 557-580
6. Reitzer, L. J., and Magasanik, B. (1985) Proc. Natl. Acad. Sci. U. S. A. 82, 1979-1983
7. Nakano, Y., Tanaka, E., Kato, C., Kimura, K., and Horikoshi, K. (1989) FEMS Microbiol. Lett. 57, 81-86
8. Sanger, F., Nicklen, S., and Coulson, A. R. (1971) Proc. Natl. Acad. Sci. U. S. A. 74, 5463-5467
9. Kempsell, K. E., Ji, Y.-E., Estrada-G, I. C. E., Colston, M. J., and Cox, R. A. (1992) J. Gen. Microbiol. 138, 1717-1727
10. Berk, A. J., and Sharp, P. A. (1977) Cell 12, 721-732
11. Amann, E., and Brosius, J. (1985) Gene (Amst.) 40, 183-190
12. Herrmann, J. L., O'Gaora, P., Gallagher, A., Thole, J. E. R., and Young, D. B. (1991) EMBO J. 15, 3547-3554
13. Thole, J. E. R., Keulen, W. J., De Bruyn, J., Kolk, A. H. J., Groothuis, D. G., Berwald, L. G., Thiesjema, R. H., and van Embden, J. D. A. (1987) Infect. Immun. 55, 1466-1475
14. Weisbrod, R. E., and Meister, A. (1973) J. Biol. Chem. 248, 3997-4002
15. Colombo, G., and Villafranca, J. J. (1986) J. Biol. Chem. 261, 10587-10591
16. Hanau, R., Koduri, R. K., Ho, N., and Brenchley, J. E. (1983) J. Bacteriol. 155, 82-89
17. Philipp, W. J., Poulet, S., Eiglmeier, K., Pascopella, L., Balasubramanian, V., Heym, B., Bergh, S., Bloom, B. R., Jacobs, W. R., Jr., and Cole, S. T. (1996) Proc. Natl. Acad. Sci. U. S. A. 93, 3132-3137
18. Ausubel, F. M. (1984) Cell 37, 5-6
19. Kimura, K., Suzuki, H., and Nakano, Y. (1989) J. Biochem. 105, 648-652
20. Backman, K., Chen, Y.-M., and Magasanik, B. (1981) Proc. Nati. Acad. Sci. U. S. A. 78, 3743-3747
21. Almassy, R. J., Janson, C. A., Hamlin, R., Xuong, N.-H., and Eisenberg, D. (1986) Nature 323, 304-309