Met23Lys mutation in subunit gamma of FOF1-ATP synthase from Rhodobacter capsulatus impairs the activation of ATP hydrolysis by protonmotive force

Biochimica et Biophysica Acta - Bioenergetics

Volumn 1767, Issue 11, 2007, Pages 1319-1330

  Feniouk, Boris A ^a   Rebecchi, Alberto ^b   Giovannini, Donatella ^b   Anefors, Sofie ^a,b   Mulkidjanian, Armen Y ^a,c   Junge, Wolfgang ^a   Turina, Paola ^b   Melandri, B Andrea ^b  

^a UNIVERSITY OF OSNABRÜCK   (Germany)

^b UNIVERSITY OF BOLOGNA   (Italy)

^c MOSCOW STATE UNIVERSITY   (Russian Federation)

Author keywords

Activation; ADP inhibition; ATP synthase; Met23Lys; Rhodobacter capsulatus; Subunit gamma

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; LYSINE; METHIONINE; PROTEIN SUBUNIT; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE;

ARTICLE; BETA CHAIN; CONTROLLED STUDY; ELECTRICITY; ENZYME ACTIVATION; ENZYME INACTIVATION; GENE MUTATION; HYDROLYSIS; MUTANT; NONHUMAN; PRIORITY JOURNAL; PROTON MOTIVE FORCE; RHODOBACTER CAPSULATUS;

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; AMINO ACID SUBSTITUTION; BACTERIAL PROTON-TRANSLOCATING ATPASES; HYDROLYSIS; KINETICS; LIGHT; MUTATION; OXIDATION-REDUCTION; PROTON PUMPS; PROTON-MOTIVE FORCE; PROTONS; PYRUVATE KINASE; RHODOBACTER CAPSULATUS;

BACTERIA (MICROORGANISMS); RHODOBACTER CAPSULATUS;

EID: 35548971136     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2007.07.009     Document Type: Article

References (68)

1. Capaldi R.A., Schulenberg B., Murray J., and Aggeler R. Cross-linking and electron microscopy studies of the structure and functioning of the Escherichia coli ATP synthase. J. Exp. Biol. 203 (2000) 29-33
2. 1-ATPase at 2.4 Å resolution. Nat. Struct. Biol. 7 (2000) 1055-1061
3. 0 complex from Escherichia coli ATP synthase. J. Bioenerg. Biomembranes 32 (2000) 357-364
4. + transport to rotary catalysis in F-type ATP synthases: structure and organization of the transmembrane rotary motor. J. Exp. Biol. 203 Pt 1 (2000) 9-17
5. 1-ATPase. Proc. Natl. Acad. Sci. U. S. A. 92 (1995) 10964-10968
6. 1-ATPase. Nature 386 (1997) 299-302
7. Sabbert D., Engelbrecht S., and Junge W. Intersubunit rotation in active F-ATPase. Nature 381 (1996) 623-625
8. 0-type ATP synthase, a biological rotary motor. Trends Biochem. Sci. 27 (2002) 154-160
9. 0-ATP synthase. FEBS Lett. 545 (2003) 61-70
10. Boyer P.D. A research journey with ATP synthase. J. Biol. Chem. 277 (2002) 39045-39061
11. Yoshida M., Muneyuki E., and Hisabori T. ATP synthase-a marvelous rotary engine of the cell. Nat. Rev., Mol. Cell Biol. 2 (2001) 669-677
12. 1 ATP synthase. Biochim. Biophys. Acta 1458 (2000) 289-299
13. Fillingame R.H., Angevine C.M., and Dmitriev O.Y. Mechanics of coupling proton movements to c-ring rotation in ATP synthase. FEBS Lett. 555 (2003) 29-34
14. i and ADP on ATPase activity in chloroplasts. Biochim. Biophys. Acta 267 (1972) 86-95
15. Fitin A.F., Vasilyeva E.A., and Vinogradov A.D. An inhibitory high affinity binding site for ADP in the oligomycin-sensitive ATPase of beef heart submitochondrial particles. Biochem. Biophys. Res. Commun. 86 (1979) 434-439
16. 1. Biochem. Biophys. Res. Commun. 89 (1979) 1300-1306
17. Feldman R.I., and Boyer P.D. The role of tightly bound ADP on chloroplast ATPase. J. Biol. Chem. 260 (1985) 13088-13094
18. Zhou J.M., Xue Z.X., Du Z.Y., Melese T., and Boyer P.D. Relationship of tightly bound ADP and ATP to control and catalysis by chloroplast ATP synthase. Biochemistry 27 (1988) 5129-5135
19. 1-ATPase and inhibits catalysis is bound at a catalytic site. Biochim. Biophys. Acta 1020 (1990) 43-48
20. Fromme P., and Gräber P. Activation/inactivation and uni-site catalysis by the reconstituted ATP- synthase from chloroplasts. Biochim. Biophys. Acta 1016 (1990) 29-42
21. 1-ATPase, is located at the catalytic site of the enzyme. FEBS Lett. 182 (1985) 419-424
22. 1. FEBS Lett. 61 (1976) 194-198
23. Gräber P., Schlodder E., and Witt H.T. Conformational change of the chloroplast ATPase induced by a transmembrane electric field and its correlation to phosphorylation. Biochim. Biophys. Acta 461 (1977) 426-440
24. Sherman P., and Wimmer M.J. Activation of ATPase of spinach coupling factor 1. Release of tightly bound ADP from the soluble enzyme. Eur. J. Biochem. 139 (1984) 367-371
25. Feniouk B.A., Mulkidjanian A.Y., and Junge W. Proton slip in the ATP synthase of Rhodobacter capsulatus: induction, proton conduction, and nucleotide dependence. Biochim. Biophys. Acta 1706 (2005) 184-194
26. Junge W. Critical electric potential difference for photophosphorylation. Its relation to the chemiosomotic hypothesis and to the triggering requirements of the ATPase system. Eur. J. Biochem. 14 (1970) 582-592
27. Melandri B.A., Baccarini-Melandri A., and Fabbri E. Energy transduction in photosynthetic bacteria. IV. Light-dependent ATPase in photosynthetic membranes from Rhodopseudomonas capsulata. Biochim. Biophys. Acta 275 (1972) 383-394
28. +-ATP synthase in the photosynthetic bacterium Rhodobacter capsulatus. J. Biol. Chem. 267 (1992) 11057-11063
29. +-ATPases from Escherichia coli or chloroplasts reconstituted into liposomes. FEBS 457 (1999) 327-332
30. 1-ATP synthase. FEBS Lett. 448 (1999) 123-126
31. Fischer S., Gräber P., and Turina P. The activity of the ATP synthase from Escherichia coli is regulated by the transmembrane proton motive force. JBC 275 (2000) 30157-30162
32. 1-ATPase in Paracoccus denitrificans plasma membranes. J. Biol. Chem. 279 (2004) 12319-12324
33. Jackson J.B., and Crofts A.R. The kinetics of light induced carotenoid changes in Rhodopseudomonas spheroides and their relation to electrical field generation across the chromatophore membrane. Eur. J. Biochem. 18 (1971) 120-130
34. Feniouk B.A., Kozlova M.A., Knorre D.A., Cherepanov D.A., Mulkidjanian A.Y., and Junge W. The proton driven rotor of ATP synthase: ohmic conductance (10 fS), and absence of voltage gating. Biophys. J. 86 (2004) 4094-4109
35. 1-ATP synthase each. Biophys. J. 82 (2002) 1115-1122
36. i. Transition state analysis of this mutant and others reveals that synthesis and hydrolysis utilize the same kinetic pathway. Biochemistry 36 (1997) 12961-12969
37. 1-ATP synthase: the uncoupling mutation, gammaM23K, disrupts the use of binding energy to drive catalysis. Biochemistry 36 (1997) 12954-12960
38. 1 ATP synthase are dependent on the energy of interaction between gamma and beta subunits. J. Biol. Chem. 272 (1997) 2300-2306
39. 1 ATP synthase by betaGlu-381 substitutions: the role of the beta380DELSEED386 segment in energy coupling. Biochem. J. 330 Pt 2 (1998) 707-712
40. 1-ATPase from wild-type or uncoupled mutant Escherichia coli. Proc. Natl. Acad. Sci. U. S. A. 96 (1999) 7780-7784
41. Lascelles J. Adaptation to form bacterichlorophyll in Rhodopseudomonas sphaeroides: changes in activity of enzymes concerned in pyrrole synthesis. Biochem. J. 72 (1959) 508-518
42. Clayton R.K. Absorption spectra of photosynthetic bacteria and their chlorophylls. In: Gest H., San Pietro A., and Vernon L.P. (Eds). Bacterial Photosynthesis (1963), The Antioch Press, Yellow Springs, OH 495-500
43. Borghese R., Crimi M., Fava L., and Melandri B.A. The ATP synthase atpHAGDC (F1) operon from Rhodobacter capsulatus. J. Bacteriol. 180 (1998) 416-421
44. Keen N.T., Tamaki S., Kobayashi D., and Trollinger D. Improved broad-host-range plasmids for DNA cloning in gram-negative bacteria. Gene 70 (1988) 191-197
45. Sharak-Genthner B.S., and Wall J.D. Ammonium uptake in Rhodopseudomonas capsulata. Arch. Microbiol. 141 (1985) 219-224
46. Solioz M., Yen H.C., and Marris B. Release and uptake of gene transfer agent by Rhodopseudomonas capsulata. J. Bacteriol. 123 (1975) 651-657
47. 1-ATP synthase is absent from about half of chromatophores. Biochim. Biophys. Acta 1506 (2001) 189-203
48. Ausländer W., and Junge W. Neutral red, a rapid indicator for pH changes in the inner phase of thylakoids. FEBS Lett. 59 2 (1975) 310-315
49. 1-complex is strongly electrogenic. FEBS Lett. 353 (1994) 189-193
50. Nishimura M., Ito T., and Chance B. Studies on bacterial photophosphorylation. III. A sensitive and rapid method of determination of photophosphorylation. Biochim. Biophys. Acta 59 (1962) 177-182
51. Nagley P., Hall R.M., and Ooi B.G. Amino acid substitutions in mitochondrial ATPase subunit 9 of Saccharomyces cerevisiae leading to oligomycin or venturicidin resistance. FEBS Lett. 195 (1986) 159-163
52. Galanis M., Mattoon J.R., and Nagley P. Amino acid substitutions in mitochondrial ATP synthase subunit 9 of Saccharomyces cerevisiae leading to venturicidin or ossamycin resistance. FEBS Lett. 249 (1989) 333-336
53. 1-ATPase complexed with the peptide antibiotic efrapeptin. Proc. Natl. Acad. Sci. U. S. A. 93 (1996) 9420-9424
54. Linnett P.E., and Beechey R.B. Inhibitors of the ATP synthetase system. Methods Enzymol. 55 (1979) 472-518
55. + translocation and phosphorylation induced by short flash excitation in Rhodopseudomonas sphaeroides chromatophores. Biochim. Biophys. Acta 408 (1975) 67-82
56. 1 under the ATP synthesis and slip conditions. FEBS Lett. 445 (1999) 409-414
57. 1-ATP synthase. Biochim. Biophys. Acta 1757 (2006) 326-338
58. 1-ATPase gamma subunit mutations perturb the coupling between catalysis and transport. J. Biol. Chem. 267 (1992) 20835-20839
59. i modulate the degree of intrinsic coupling in the ATP synthase of the photosynthetic bacterium Rhodobacter capsulatus. Biochemistry 43 (2004) 11126-11134
60. 1 motor by external force. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 4288-4293
61. 1-ATPase from bovine heart mitochondria. Nature 370 (1994) 621-628
62. 2+ ADP and aluminium fluoride. Struct. Fold. Des. 8 (2000) 567-573
63. 1-ATPase with nucleotide bound to all three catalytic sites: implications for the mechanism of rotary catalysis. Cell 106 (2001) 331-341
64. 1-ATPase are not influenced by crystallisation at high concentrations of nucleotide. FEBS Lett. 494 (2001) 11-14
65. Kagawa R., Montgomery M.G., Braig K., Leslie A.G.W., and Walker J.E. The structure of bovine F-1-ATPase inhibited by ADP and beryllium fluoride. EMBO J. 23 (2004) 2734-2744
66. Bowler M.W., Montgomery M.G., Leslie A.G., and Walker J.E. How azide inhibits ATP hydrolysis by the F-ATPases. Proc. Natl. Acad. Sci. U. S. A. 103 (2006) 8646-8649
67. 1-ATPase during catalysis. Proc. Natl. Acad. Sci. U. S. A. 98 (2001) 13649-13654
68. 1-ATPase lower ATPase activity by disrupting a cluster of hydrophobic side chains. Biochemistry 43 (2004) 9495-9501