Heterologous expression of correctly assembled methylamine dehydrogenase in Rhodobacter sphaeroides

Journal of Bacteriology

Volumn 181, Issue 14, 1999, Pages 4216-4222

  Graichen, M Elizabeth ^a   Jones, Limei H ^a   Sharma, Bethel V ^a   Van Spanning, Rob J M ^b   Hosler, Jonathan P ^a   Davidson, Victor L ^a  

^a UNIVERSITY OF MISSISSIPPI MEDICAL CENTER   (United States)

^b VU UNIVERSITY AMSTERDAM   (Netherlands)

Author keywords

[No Author keywords available]

Indexed keywords

AMICYANIN; AMINE DEHYDROGENASE; BACTERIAL PROTEIN; CARBON; GENE PRODUCT; STRUCTURAL PROTEIN; TRYPTOPHAN TRYPTOPHYLQUINONE; UNCLASSIFIED DRUG;

ARTICLE; BACTERIAL GENE; CONTROLLED STUDY; CYTOPLASM; DISULFIDE BOND; ESCHERICHIA COLI; GENE EXPRESSION; NONHUMAN; PARACOCCUS DENITRIFICANS; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN TRANSPORT; RHODOBACTER SPHAEROIDES;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; PARACOCCUS DENITRIFICANS; RHODOBACTER SPHAEROIDES; RHODOPSEUDOMONAS;

EID: 0032788792     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.181.14.4216-4222.1999     Document Type: Article

References (34)

1. Alefounder, P. R., and S. J. Ferguson. 1980. The location of dissimilatory nitrite reductase and the control of dissimilatory nitrate reductase by oxygen in Paracoccus denitrificans. Biochem. J. 192:231-240.
2. Barber, R. D., and T. J. Donohue. 1998. Function of a glutathione-dependent formaldehyde dehydrogenase in Rhodobacter sphaeroides formaldehyde oxidation and assimilation. Biochemistry 37:530-537.
3. Berks, B. C. 1996. A common export pathway for proteins binding complex redox cofactors. Mol. Microbiol. 22:393-404.
4. Bishop, G. R., H. B. Brooks, and V. L. Davidson. 1996. Evidence for a tryptophan tryptophylquinone aminosemiquinone intermediate in the physiologic reaction between methylamine dehydrogenase and amicyanin. Biochemistry 35:8948-8954.
5. Brooks, H. B., and V. L. Davidson. 1994. Kinetic and thermodynamic analysis of a physiologic intermolecular electron transfer reaction between methylamine dehydrogenase and amicyanin. Biochemistry 33:5696-5701.
6. Brooks, H. B., L. H. Jones, and V. L. Davidson. 1993. Stopped-flow kinetic and deuterium kinetic isotope effect studies of the quinoprotein methylamine dehydrogenase from Paracoccus denitrificans. Biochemistry 32:2725-2729.
7. Cao, J., J. Shapleigh, R. Gennis, A. Rezvin, and S. Ferguson-Miller. 1991. The gene encoding cytochrome c oxidase subunit II from Rhodobacter sphaeroides; comparison of the deduced amino acid sequence with sequences of corresponding peptides from other species. Gene 101:133-137.
8. Chang, J. P., and J. G. Morris. 1962. Studies on the utilization of nitrate by Micrococcus denitrificans. J. Gen. Microbiol. 29:301-310.
9. Chistoserdov, A., C. Boyd, F. S. Mathews, and M. E. Lidstrom. 1992. The genetic organization of the mau gene cluster of the facultative autotroph Paracoccus denitrificans. Biochem. Biophys. Res. Commun. 184:1181-1189.
10. Chistoserdov, A. Y., L. V. Chistoserdova, W. S. McIntire, and M. E. Lidstrom. 1994. Genetic organization of the mau gene cluster in Methylobacterium extorquens AM1: complete nucleotide sequence and generation and characteristics of mau mutants. J. Bacteriol. 176:4052-4065.
11. Chung, C. T., and R. H. Miller. 1993. Preparation and storage of competent E. coli cells. Methods Enzymol. 218:621-627.
12. Davidson, V. L. 1990. Methylamine dehydrogenases from methylotrophic bacteria. Methods Enzymol. 188:241-246.
13. Davidson, V. L. 1993. Methylamine dehydrogenase, p. 73-95. In V. L. Davidson (ed.), Principles and applications of quinoproteins. Marcel Dekker, New York, N.Y.
14. Davidson, V. L., H. B. Brooks, M. E. Graichen, L. H. Jones, and Y.-L. Hyun. 1995. Detection of intermediates in TTQ enzymes. Methods Enzymol. 258: 176-190.
15. Davidson, V. L., L. H. Jones, M. E. Graichen, F. S. Mathews, and J. P. Hosler. 1997. Factors which stabilize the methylamine dehydrogenase-amicyanin electron transfer complex revealed by site-directed mutagenesis. Biochemistry 36:12733-12738.
16. DeVries, G. E., N. Harms, J. Hoogendijk, and A. H. Stouthamer. 1989. Isolation and characterization of Paracoccus denitrificans mutants with increased conjugation frequencies and pleiotropic loss of a n(GATC)n DNA-modifying property. Arch. Microbiol. 152:52-57.
17. Fairburn, C., and J. P. Hosler. Unpublished data.
18. Flory, J. E., and T. J. Donohue. 1997. Transcriptional control of several aerobically induced cytochrome structural genes in Rhodobacter sphaeroides. Microbiology 143:3101-3110.
19. Govindarai, S., E. Eisenstein, L. H. Jones, L. Sanders-Loehr, A. Y. Chistoserdov, V. L. Davidson, and S. L. Edwards. 1994. Aromatic amine dehydrogenase, a second tryptophan tryptophylquinone enzyme. J. Bacteriol. 176:2922-2929.
20. Husain, M., and V. L. Davidson. 1985. An inducible periplasmic blue copper protein from Paracoccus denitrificans. Purification, properties and physiological role. J. Biol. Chem. 260:14626-14629.
21. Husain, M., and V. L. Davidson. 1987. Purification and properties of methylamine dehydrogenase from Paracoccus denitrificans. J. Bacteriol. 169:1712-1717.
22. Keen, N. T., S. Tamaki, D. Kobayashi, and D. Trollinger. 1988. Improved broad-host-range plasmids for DNA cloning in Gram-negative bacteria. Gene 70:191-197.
23. McIntire, W. S., D. E. Wemmer, A. Y. Chistoserdov, and M. E. Lidstrom. 1991. A new cofactor in a prokaryotic enzyme: tryptophan tryptophylquinone as the redox prosthetic group in methylamine dehydrogenase. Science 252: 817-824.
24. Quayle, J. R., and N. Pfennig. 1975. Utilization of methanol by Rhodospirillaceae. Arch. Microbiol. 102:193-198.
25. Sambrook, J., E. F. Fritsch, and T. Maniatis. 1989. Molecular cloning: a laboratory manual, 2nd ed. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
26. Sargent, F., E. G. Bogsch, N. R. Stanley, M. Wexler, C. Robinson, B. C. Berks, and T. Palmer. 1998. Overlapping functions of components of a bacterial Sec-independent protein export pathway. EMBO J. 17:3640-3650.
27. Simon, R., U. Priefer, and A. Puhler. 1983. A broad host range mobilization system for in vivo genetic engineering: transposon mutagenesis in Gram negative bacteria. Bio/Technology 1:784-791.
28. Sistrom, W. R. 1960. A requirement for sodium in the growth of Rhodopseudomonas sphaeroides. J. Gen. Microbiol. 22:778-785.
29. Van der Palen, C. J., D. J. Slotboom, L. Jongejan, W. N. Reijnders, N. Harms, J. A. Duine, and R. J. Van Spanning. 1995. Mutational analysis of mau genes involved in methylamine metabolism in Paracoccus denitrificans. Eur. J. Biochem. 230:860-871.
30. Van der Palen, C. J., W. N. Reijnders, S. de Vries, J. A. Duine, and R. J. Van Spanning. 1997. MauE and MauD proteins are essential in methylamine metabolism of Paracoccus denitrificans. Antonie Leeuwenhoek 72:219-228.
31. Van Spanning, R. J., C. W. Wansell, W. N. Readers, L. F. Oltmann, and A. H. Stouthamer. 1990. Mutagenesis of the gene encoding amicyanin of Paracoccus denitrificans and the resultant effect on methylamine oxidation. FEBS Lett. 275:217-220.
32. Van Spanning, R. J., C. J. Van der Palen, D. J. Slotboom, W. N. Reijnders, A. H. Stouthamer, and J. A. Duine. 1994. Expression of the mau genes involved in methylamine metabolism in Paracoccus denitrificans is under the control of a LysR-type transcriptional activator. Eur. J. Biochem. 226:201-210.
33. Woese, C. R. 1987. Bacterial evolution. Microbiol. Rev. 51:221-271.
34. Zhu, Z., and V. L. Davidson. 1998. Redox properties of tryptophan tryptophylquinone enzymes. Correlation with structure and reactivity. J. Biol. Chem. 273:14254-14260.