Unexpected elevated production of Aquifex aeolicus cytochrome c 555 in Escherichia coli cells lacking disulfide oxidoreductases

Bioscience, Biotechnology and Biochemistry

Volumn 69, Issue 7, 2005, Pages 1418-1421

  Kojima, Nobusuke ^a   Yamanaka, Masaru ^a   Ichiki, Shin Ichi ^a   Sambongi, Yoshihiro ^a  

^a HIROSHIMA UNIVERSITY   (Japan)

Author keywords

Aquifex aeolicus; Cytochrome c production; Hyperthermophile; Thiol disulfide redox control

Indexed keywords

BACTERIA; CELLS; ENZYMES; ESCHERICHIA COLI; REDOX REACTIONS;

AQUIFLEX AEOLICUS; CYTOCHROME C PRODUCTION; DISULFIDE BOND FORMATION; HYPERTHERMOPHILE; MUTANT STRAINS; THIOL-DISULFIDE REDOX CONTROL;

BIOCHEMISTRY;

BACTERIAL PROTEIN; CYTOCHROME C; CYTOCHROME C 555; CYTOCHROME C-555; MEMBRANE PROTEIN; OXIDOREDUCTASE; PROTEIN DISULFIDE ISOMERASE; RECOMBINANT PROTEIN;

AMINO ACID SEQUENCE; ARTICLE; COMPARATIVE STUDY; ESCHERICHIA COLI; GENETICS; METABOLISM; MUTATION; POLYACRYLAMIDE GEL ELECTROPHORESIS;

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; CYTOCHROME C GROUP; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ESCHERICHIA COLI; MEMBRANE PROTEINS; MUTATION; OXIDOREDUCTASES; PROTEIN DISULFIDE-ISOMERASE; RECOMBINANT PROTEINS;

AQUIFEX AEOLICUS; ESCHERICHIA COLI;

EID: 23944497157     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.69.1418     Document Type: Article

References (23)

1. Page, M. D., Sambongi, Y., and Ferguson, S. J., Contrasting routes of c-type cytochrome assembly in mitochondria, chloroplast and bacteria. Trends Biochem. Sci., 23, 103-108 (1998).
2. Sambongi, Y., Uchiyama, S., Kobayashi, Y., Igarashi, Y., and Hasegawa, J., Cytochrome c from a thermophilic bacterium has provided insights into the mechanism of protein maturation, folding, and stability. Eur. J. Biochem., 269, 3355-3361 (2002).
3. Thöny-Meyer, L., Cytochrome c maturation: a complex pathway for a simple task? Biochem. Soc. Trans., 30, 633-638 (2002).
4. Sanders, C., and Lill, H., Expression of prokaryotic and eukaryotic cytochromes c in Escherichia coli. Biochim. Biophys. Acta, 1459, 131-138 (2000).
5. Rietsch, A., Bessette, P., Georgiou, G., and Beckwith, J., Reduction of the periplasmic disulfide bond isomerase, DsbC, occurs by passage of electrons from cytoplasmic thioredoxin. J. Bacteriol., 179, 6602-6608 (1997).
6. 552. J. Biol. Chem., 274, 37533-37537 (1999).
7. 552 from a moderate thermophilic bacterium, Hydrogenophilus thermoluteolus. Acta Cryst., F61, 395-398 (2005).
8. 552: reciprocal mutation analysis. J. Biol. Chem., 280, 5527-5532 (2005).
9. s and investigation of the role of methionine residues. Biochemistry, 40, 13690-13698 (2001).
10. Tanaka, Y., Ashikari, T., Shibano, Y., Amachi, T., Yoshizumi, H., and Matsubara, H., Construction of a human cytochrome c gene and its functional expression in Saccharomyces cerevisiae. J. Biochem. (Tokyo), 103, 954-961 (1988).
11. 6 and plastocyanin in Arabidopsis. Nature, 417, 567-571 (2002).
12. Zhang, Y., Arai, H., Sambongi, Y., Igarashi, Y., and Kodama, T., Heterologous expression of Hydrogenobacter thermophilus cytochrome c-552 in the periplasm of Pseudomonas aeruginosa. J. Ferment. Bioeng., 85, 346-349 (1998).
13. 552 does not: implications for c-type cytochrome biogenesis. FEBS Lett., 340, 65-70 (1994).
14. 550 probes pathway of c-type cytochrome biogenesis in Escherichia coli. Mol. Microbiol., 19, 1193-1204 (1996).
15. Goodhew, C. F., Brown, K. R., and Pettigrew, G. W., Haem staining in gels, a useful tool in the study of bacterial c-type cytochromes. Biochim. Biophys. Acta, 852, 288-294 (1986).
16. 552. FEBS Lett., 344, 207-210 (1994).
17. Sambongi, Y., and Ferguson, S. J., Mutants of Escherichia coli lacking disulphide oxidoreductases DsbA and DsbB cannot synthesise an exogenous monohaem c-type cytochrome except in the presence of disulphide compounds. FEBS Lett., 398, 265-268 (1996).
18. Allen, J. W., Daltrop, O., Stevens, J. M., and Ferguson, S. J., C-type cytochromes: diverse structures and biogenesis systems pose evolutionary problems. Philos. Trans. R. Soc. Lond. B Biol. Sci., 358, 255-266 (2003).
19. Akiyama, S., Takahashi, S., Ishimori, K., and Morishima, I., Stepwise formation of α-helices during cytochrome c folding. Nat. Struct. Biol., 7, 514-520 (2000).
20. Sanbongi, Y., Yang, J. H., Igarashi, Y., and Kodama, T., Cloning, nucleotide sequence and expression of the cytochrome c-552 gene from Hydrogenobacter thermophilus. Eur. J. Biochem., 198, 7-12 (1991).
21. 552 retains its native structure. J. Biol. Chem., 279, 15177-15182 (2004).
22. Sanbongi, Y., Igarashi, Y., and Kodama, T., Thermostability of cytochrome c-552 from the thermophilic hydrogen-oxidizing bacterium Hydrogenobacter thermophilus. Biochemistry, 28, 9574-9578 (1989).
23. Deckert, G., Warren, P. V., Gaasterland, T., Young, W. G., Lenox, A. L., Graham, D. E., Overbeek, R., Snead, M. A., Keller, M., Aujay, M., Huber, R., Feldman, R. A., Short, J. M., Olsen, G. J., and Swanson, R. V., The complete genome of the hyperthermophilic bacterium Aquifex aeolicus. Nature, 392, 353-358 (1998).