Temperature adaptation of Bacillus subtilis by chromosomal groEL replacement

Bioscience, Biotechnology and Biochemistry

Volumn 70, Issue 10, 2006, Pages 2357-2362

  Endo, Ayako ^a   Sasaki, Mayumi ^a   Maruyama, Akihiko ^b   Kurusu, Yasurou ^a  

^a IBARAKI UNIVERSITY   (Japan)

^b NATIONAL INSTITUTE OF ADVANCED INDUSTRIAL SCIENCE AND TECHNOLOGY AIST   (Japan)

Author keywords

Bacillus subtilis; GroEL; Mutator; Temperature adaptation

Indexed keywords

AMINO ACIDS; MONOMERS; MUTAGENESIS; SUBSTITUTION REACTIONS; THERMAL EFFECTS;

BACILLUS SUBTILIS; MUTATOR; TEMPERATURE ADAPTATION;

BACTERIA;

ADENOSINE TRIPHOSPHATE; CHAPERONIN;

ADAPTATION; AMINO ACID SUBSTITUTION; ARTICLE; BACILLUS SUBTILIS; BINDING SITE; GENETIC SELECTION; GENETICS; METABOLISM; MUTAGENESIS; PHYSIOLOGY; TEMPERATURE;

ADAPTATION, PHYSIOLOGICAL; ADENOSINE TRIPHOSPHATE; AMINO ACID SUBSTITUTION; BACILLUS SUBTILIS; BINDING SITES; GROEL PROTEIN; MUTAGENESIS; SELECTION (GENETICS); TEMPERATURE;

BACILLUS SUBTILIS; BACTERIA (MICROORGANISMS);

EID: 33750435188     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.50689     Document Type: Article

References (18)

1. Frydman, J., Folding of newly translated proteins in vivo: the role of molecular chaperones. Ann. Rev. Biochem., 70, 603-647 (2001).
2. Braig, K., Otwinowski, Z., Hegde, R., Boisvert, D. C., Joachimiak, A., Horwich, A. L., and Sigler, P. B., The crystal structure of the bacterial chaperonin GroEL at 2.8 angstrom. Nature, 371, 578-586 (1994).
3. Hunt, J. F., Weaver, A. J., Landry, S. J., Gierasch, L., and Deisenhofer, J., The crystal structure of the GroES co-chaperonin at 2.8 angstrom. Nature, 379, 37-45 (1996).
4. Maruyama, A., Honda, D., Yamamoto, H., Kitamura, K., and Higashihara, T., Phylogenetic analysis of psychrophilic bacteria isolated from the Japan Trench, including a description of the deep-sea species Psychrobacter pacificensis sp. nov. Int. J. Syst. Evol. Microbiol., 50, 835-846 (2000).
5. Hemmingsen, S. M., Woolford, C., van der Vies, S. M., Tilly, K., Dennis, D. T., Georgopoulos, C. P., Hendrix, R. W., and Ellis, J., Homologous plant and bacterial proteins chaperone oligomeric protein assembly. Nature, 333, 330-334 (1988).
6. Fleury, A. M., Shazand, K., Frandsen, N., and Stragier, P., Antibiotic-resistance cassette for Bacillus subtilis. Gene, 167, 335-336 (1995).
7. Leighton, T. J., and Doi, R. H., The stability of messenger ribonucleic acid during sporulation in Bacillus subtilis. J. Biol. Chem., 254, 3189-3195 (1971).
8. Li, M., and Wong, S. L., Cloning and characterization of the groESL operon from Bacillus subtilis. J. Bacteriol., 174, 3981-3992 (1992).
9. Schaeffer, P., Millet, J., and Aubert, J. P., Catabolic repression of bacterial sporulation. Proc. Natl. Acad. Sci. USA, 54, 704-711 (1965).
10. Sasaki, M., Yonemura, Y., and Kurusu, Y., Genetic analysis of Bacillus subtilis mutator genes. J. Gen. Appl. Microbiol., 46, 183-187 (2000).
11. Sasaki, M., and Kurusu, Y., Analysis of spontaneous base substitutions generated in mutator strain of Bacillus subtilis. FEMS Microbiol. Lett., 234, 37-42 (2004).
12. Mendoza, J. A., Rogers, E., Lorimer, G. H., and Horowitz, P. M., Chaperonins facilitate the in vitro folding of monomeric mitochondrial rhodanese. J. Biol. Chem., 266, 13044-13049 (1991).
13. Martin, J., Langer, T., Boteva, R., Schramel, A., Horwich, A. L., and Hartl, F. U., Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate. Nature, 352, 36-42 (1991).
14. Nakamura, T., Tanaka, M., Maruyama, A., Higashi, Y., and Kurusu, Y., A nonconserved carboxy-terminal segment of GroEL contributes to reaction temperature. Biosci. Biotechnol. Biochem., 68, 2498-2504 (2004).
15. Mizobata, T., Akiyama, Y., Ito, K., Yumoto, N., and Kawata, Y., Effects of the chaperonin GroE on the refolding of tryptophanase from Escherichia coli. J. Biol. Chem., 267, 17773-17779 (1992).
16. Ferrer, M., Lunsdorf, H., Chernikova, T. N., Yakimov, M., Timmis, K. N., and Golyshin, P. N., Functional consequences of single:double ring transitions in chaperonins: life in the cold. Mol. Microbiol., 53, 167-182 (2004).
17. Ferrer, M., Chernikova, T. N., Yakimov, M., Golyshin, P. N., and Timmis, K. N., Chaperonins govern growth of Escherichia coli at low temperatures. Nat. Biotechnol., 21, 1266-1267 (2003).
18. Sun, Z., Scott, D. J., and Lund, P. A., Isolation and characterization of mutants of GroEL that are fully functional as single rings. J. Mol. Biol., 332, 715-728 (2003).