The ATP synthase a-subunit of extreme alkaliphiles is a distinct variant: Mutations in the critical alkaliphile-specific residue Lys-180 and other residues that support alkaliphile oxidative phosphorylation

Journal of Biological Chemistry

Volumn 285, Issue 42, 2010, Pages 32105-32115

  Fujisawa, Makoto ^a,b   Fackelmayer, Oliver J ^a   Liu, Jun ^a   Krulwich, Terry A ^a   Hicks, David B ^a  

^a MOUNT SINAI SCHOOL OF MEDICINE   (United States)

^b TOYO UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

ALKALIPHILE; ATP SYNTHASE; ATP SYNTHESIS; ATP-ASE ACTIVITY; BACILLUS PSEUDOFIRMUS; BACILLUS SPECIES; HIGH PH; IN-VITRO; LYSINE RESIDUES; OXIDATIVE PHOSPHORYLATION; PROTON UPTAKE; PROTON-MOTIVE FORCES; SYNTHASES; UNCOUPLERS; WILD TYPES;

BACTERIOLOGY; PHOSPHORYLATION; PROTONS;

AMINO ACIDS;

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; ALANINE; ARGININE; CYSTEINE; GLYCINE; HISTIDINE; LYSINE; MALIC ACID; MUTANT PROTEIN; PROTON; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATASE; SYNTHETASE; THERMOALKALIPHILE SYNTHASE; UNCLASSIFIED DRUG;

ALKALINITY; AMINO ACID SUBSTITUTION; ARTICLE; BACILLUS; BACILLUS PSEUDOFIRMUS; BACTERIAL CHROMOSOME; BACTERIAL GROWTH; BACTERIAL METABOLISM; BACTERIUM MUTANT; CONTROLLED STUDY; ENZYME ACTIVATION; ENZYME ACTIVITY; ENZYME SUBUNIT; NONHUMAN; NUCLEOTIDE SEQUENCE; OXIDATIVE PHOSPHORYLATION; PRIORITY JOURNAL; PROTEIN VARIANT; WILD TYPE;

ADENOSINE TRIPHOSPHATASES; ADENOSINE TRIPHOSPHATE; AMINO ACID SEQUENCE; ATP SYNTHETASE COMPLEXES; BACILLUS; BACTERIAL PROTEINS; HYDROGEN-ION CONCENTRATION; ISOENZYMES; LYSINE; MOLECULAR SEQUENCE DATA; MUTATION; OXIDATIVE PHOSPHORYLATION; PROTEIN CONFORMATION; PROTEIN SUBUNITS; SEQUENCE ALIGNMENT;

BACILLUS PSEUDOFIRMUS;

EID: 77957781806     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M110.165084     Document Type: Article

References (62)

1. Mitchell, P. (1961) Nature 191, 144-148
2. Stock, D., Gibbons, C., Arechaga, I., Leslie, A. G., and Walker, J. E. (2000) Curr. Opin. Struct. Biol. 10, 672-679
3. von Ballmoos, C., Cook, G. M., and Dimroth, P. (2008) Annu. Rev. Biophys. 37, 43-64
4. Fillingame, R. H., Angevine, C. M., and Dmitriev, O. Y. (2003) FEBS Lett. 555, 29-34
5. von Ballmoos, C., Wiedenmann, A., and Dimroth, P. (2009) Annu. Rev. Biochem. 78, 649-672
6. Yoshida, M., Muneyuki, E., and Hisabori, T. (2001) Nat. Rev. Mol. Cell Biol. 2, 669-677
7. Nakamoto, R. K., Baylis Scanlon, J. A., and Al-Shawi, M. K. (2008) Arch. Biochem. Biophys. 476, 43-50
8. Nakanishi-Matsui, M., Sekiya, M., Nakamoto, R. K., and Futai, M. (2010) Biochim. Biophys. Acta 1797, 1343-1352
9. Nishizaka, T., Oiwa, K., Noji, H., Kimura, S., Muneyuki, E., Yoshida, M., and Kinosita, K., Jr. (2004) Nat. Struct. Mol. Biol. 11, 142-148
10. Ueno, H., Suzuki, T., Kinosita, K., Jr., and Yoshida, M. (2005) Proc. Natl. Acad. Sci. U.S.A. 102, 1333-1338
11. Jiang, W., Hermolin, J., and Fillingame, R. H. (2001) Proc. Natl. Acad. Sci. U.S.A. 98, 4966-4971
12. Meier, T., Morgner, N., Matthies, D., Pogoryelov, D., Keis, S., Cook, G. M., Dimroth, P., and Brutschy, B. (2007) Mol. Microbiol. 65, 1181-1192
13. Meier, T., Polzer, P., Diederichs, K., Welte, W., and Dimroth, P. (2005) Science 308, 659-662
14. Pogoryelov, D., Reichen, C., Klyszejko, A. L., Brunisholz, R., Muller, D. J., Dimroth, P., and Meier, T. (2007) J. Bacteriol. 189, 5895-5902
15. Pogoryelov, D., Yu, J., Meier, T., Vonck, J., Dimroth, P., and Muller, D. J. (2005) EMBO Rep. 6, 1040-1044
16. Stock, D., Leslie, A. G., and Walker, J. E. (1999) Science 286, 1700-1705
17. Angevine, C. M., Herold, K. A., and Fillingame, R. H. (2003) Proc. Natl. Acad. Sci. U.S.A. 100, 13179-13183
18. Angevine, C. M., Herold, K. A., Vincent, O. D., and Fillingame, R. H. (2007) J. Biol. Chem. 282, 9001-9007
19. Langemeyer, L., and Engelbrecht, S. (2007) Biochim. Biophys. Acta 1767, 998-1005
20. Moore, K. J., Angevine, C. M., Vincent, O. D., Schwem, B. E., and Fillingame, R. H. (2008) J. Biol. Chem. 283, 13044-13052
21. Moore, K. J., and Fillingame, R. H. (2008) J. Biol. Chem. 283, 31726-31735
22. Schwem, B. E., and Fillingame, R. H. (2006) J. Biol. Chem. 281, 37861-37867
23. Steed, P. R., and Fillingame, R. H. (2008) J. Biol. Chem. 283, 12365-12372
24. Steed, P. R., and Fillingame, R. H. (2009) J. Biol. Chem. 284, 23243-23250
25. Mitome, N., Ono, S., Sato, H., Suzuki, T., Sone, N., and Yoshida, M. (2010) Biochem. J. 430, 171-177
26. Aksimentiev, A., Balabin, I. A., Fillingame, R. H., and Schulten, K. (2004) Biophys. J. 86, 1332-1344
27. Elston, T., Wang, H., and Oster, G. (1998) Nature 391, 510-513
28. Lau, W. C., and Rubinstein, J. L. (2010) Proc. Natl. Acad. Sci. U.S.A. 107, 1367-1372
29. Dimroth, P., and Cook, G. M. (2004) Adv. Microb. Physiol. 49, 175-218
30. Hicks, D. B., Liu, J., Fujisawa, M., and Krulwich, T. A. (2010) Biochim. Biophys. Acta 1797, 1362-1377
31. Preiss, L., Yildiz, O., Hicks, D. B., Krulwich, T. A., and Meier, T. (2010) PLoS Biol. 8, e1000443
32. Krulwich, T. A. (1995) Mol. Microbiol. 15, 403-410
33. Krulwich, T. A., Hicks, D. B., Swartz, T. H., and Ito, M. (2007) in Physiology and Biochemistry of Extremophiles (Gerday, C., and Glansdorff, N., eds) pp. 311-329, ASM Press, Washington, DC
34. Sturr, M. G., Guffanti, A. A., and Krulwich, T. A. (1994) J. Bacteriol. 176, 3111-3116
35. Ivey, D. M., and Krulwich, T. A. (1992) Res. Microbiol. 143, 467-470
36. Liu, J., Fujisawa, M., Hicks, D. B., and Krulwich, T. A. (2009) J. Biol. Chem. 284, 8714-8725
37. Wang, Z., Hicks, D. B., Guffanti, A. A., Baldwin, K., and Krulwich, T. A. (2004) J. Biol. Chem. 279, 26546-26554
38. McMillan, D. G., Keis, S., Dimroth, P., and Cook, G. M. (2007) J. Biol. Chem. 282, 17395-17404
39. McMillan, D. G., Keis, S., Berney, M., and Cook, G. M. (2009) Appl. Environ. Microbiol. 75, 7649-7654
40. Hartzog, P. E., and Cain, B. D. (1994) J. Biol. Chem. 269, 32313-32317
41. Ito, M., Guffanti, A. A., Zemsky, J., Ivey, D. M., and Krulwich, T. A. (1997) J. Bacteriol. 179, 3851-3857
42. Lowry, O. H., Rosebrough, N. J., Farr, A. L., and Randall, R. J. (1951) J. Biol. Chem. 193, 265-275
43. Chan, K. M., Delfert, D., and Junger, K. D. (1986) Anal. Biochem. 157, 375-380
44. Maehama, T., Taylor, G. S., Slama, J. T., and Dixon, J. E. (2000) Anal. Biochem. 279, 248-250
45. Rowlands, M. G., Newbatt, Y. M., Prodromou, C., Pearl, L. H., Workman, P., and Aherne, W. (2004) Anal. Biochem. 327, 176-183
46. Schägger, H., and von Jagow, G. (1987) Anal. Biochem. 166, 368-379
47. Nesterenko, M. V., Tilley, M., and Upton, S. J. (1994) J. Biochem. Biophys. Methods 28, 239-242
48. Vorburger, T., Ebneter, J. Z., Wiedenmann, A., Morger, D., Weber, G., Diederichs, K., Dimroth, P., and von Ballmoos, C. (2008) FEBS J. 275, 2137-2150
49. Stanley, P. E., and Williams, S. G. (1969) Anal. Biochem. 29, 381-392
50. Ono, S., Sone, N., Yoshida, M., and Suzuki, T. (2004) J. Biol. Chem. 279, 33409-33412
51. Hicks, D. B., and Krulwich, T. A. (1990) J. Biol. Chem. 265, 20547-20554
52. Cain, B. D., and Simoni, R. D. (1989) J. Biol. Chem. 264, 3292-3300
53. DeLeon-Rangel, J., Zhang, D., and Vik, S. B. (2003) Arch. Biochem. Biophys. 418, 55-62
54. Liu, J., Fackelmayer, O., Preiss, L., Meier, T., Hicks, D. B., and Krulwich, T. A. (2010) Biochim. Biophys. Acta 1797S, 35-36
55. Rath, A., Glibowicka, M., Nadeau, V. G., Chen, G., and Deber, C. M. (2009) Proc. Natl. Acad. Sci. U.S.A. 106, 1760-1765
56. Gilmour, R., and Krulwich, T. A. (1997) J. Bacteriol. 179, 863-870
57. Quirk, P. G., Guffanti, A. A., Plass, R. J., Clejan, S., and Krulwich, T. A. (1991) Biochim. Biophys. Acta 1058, 131-140
58. Quirk, P. G., Hicks, D. B., and Krulwich, T. A. (1993) J. Biol. Chem. 268, 678-685
59. Stocker, A., Keis, S., Vonck, J., Cook, G. M., and Dimroth, P. (2007) Structure 15, 904-914
60. Angevine, C. M., and Fillingame, R. H. (2003) J. Biol. Chem. 278, 6066-6074
61. Jiang, W., and Fillingame, R. H. (1998) Proc. Natl. Acad. Sci. U.S.A. 95, 6607-6612
62. Vik, S. B., and Ishmukhametov, R. R. (2005) J. Bioenerg. Biomembr. 37, 445-449