Biochemical and molecular characterization of a Na+- translocating F1Fo-ATPase from the thermoalkaliphilic bacterium Clostridium paradoxum

Journal of Bacteriology

Volumn 188, Issue 14, 2006, Pages 5045-5054

  Ferguson, Scott A ^a   Keis, Stefanie ^a   Cook, Gregory M ^a,b  

^a UNIVERSITY OF OTAGO   (New Zealand)

^b UNIVERSITY OF OTAGO   (New Zealand)

Author keywords

[No Author keywords available]

Indexed keywords

PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; TRICHLOROACETIC ACID;

ARTICLE; BACTERIUM IDENTIFICATION; CARBOXY TERMINAL SEQUENCE; CLOSTRIDIUM; CLOSTRIDIUM PARADOXUM; ELECTRIC POTENTIAL; ELECTROCHEMICAL ANALYSIS; ENZYME ANALYSIS; ENZYME PURIFICATION; MEMBRANE BINDING; MEMBRANE POTENTIAL; MOLECULAR CLONING; NONHUMAN; NUCLEOTIDE SEQUENCE; OLIGOMERIZATION; OPERON; PRIORITY JOURNAL; PROTEIN MOTIF; THERMOPHILIC BACTERIUM;

ADENOSINE TRIPHOSPHATASES; AMINO ACID SEQUENCE; BACTERIAL PROTEINS; CATION TRANSPORT PROTEINS; CLOSTRIDIUM; CONSERVED SEQUENCE; DICYCLOHEXYLCARBODIIMIDE; HEAT; KINETICS; MOLECULAR SEQUENCE DATA; PROTEIN SUBUNITS; PROTON-TRANSLOCATING ATPASES; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID; SODIUM CHLORIDE; THERMODYNAMICS;

BACTERIA (MICROORGANISMS); CLOSTRIDIUM PARADOXUM;

EID: 33745882947     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.00128-06     Document Type: Article

References (59)

1. 1-ATPase from bovine heart mitochondria. Nature 370:621-628.
2. Church, G. M., and W. Gilbert. 1984. Genomic sequencing. Proc. Natl. Acad. Sci. USA 81:1991-1995.
3. Cipriano, D. J., and S. D. Dunn. 2006. The role of the ε subunit in the Escherichia coli ATP synthase. The C-terminal domain is required for efficient energy coupling. J. Biol. Chem. 281:501-507.
4. o-ATP synthase from thermoalkaliphilic Bacillus sp. strain TA2.A1. J. Bacteriol. 185:4442-4449.
5. Cook, G. M., J. B. Russell, A. Reichert, and J. Wiegel. 1996. The intracellular pH of Clostridium paradoxum, an anaerobic, alkaliphilic, and thermophilic bacterium. Appl. Environ. Microbiol. 62:4576-4579.
6. Cotter, P. D., and C. Hill. 2003. Surviving the acid test: responses of gram-positive bacteria to low pH. Microbiol. Mol. Biol. Rev. 67:429-453.
7. o ATP synthase: operon, composition, and some properties. J. Bacteriol. 185:5527-5535.
8. o complex. Annu. Rev. Microbiol. 50:791-824.
9. +-coupled ATP synthases operating at low electrochemical potential. Adv. Microb. Physiol. 49:175-218.
10. Dimroth, P., C. von Ballmoos, T. Meier, and G. Kaim. 2003. Electrical power fuels rotary ATP synthase. Structure 11:1469-1473.
11. o ATP synthase: model derived from solution structure of the monomer and cross-linking in the native enzyme. Proc. Natl. Acad. Sci. USA 96:7785-7790.
12. 1): biochemical and molecular biological approaches. Microbiol. Rev. 47:285-312.
13. Hanahan, D., J. Jessee, and F. R. Bloom. 1991. Plasmid transformation of Escherichia coli and other bacteria. Methods Enzymol. 204:63-113.
14. +. J. Biol. Chem. 265:20547-20554.
15. Hoffmann, A., and P. Dimroth. 1991. The ATPase at Bacillus alcalophilus. Reconstitution of energy-transducing functions. Eur. J. Biochem. 196:493-497.
16. Hoffmann, A., and P. Dimroth. 1991. The electrochemical proton potential of Bacillus alcalophilus. Eur. J. Biochem. 201:467-473.
17. o-ATPase complex in the thermophilic bacterium Clostridium fervidus. J. Bacteriol. 179:1274-1279.
18. Iida, T., K. Inatomi, Y. Kamagata, and T. Maruyama. 2002. F- and V-type ATPases in the hyperthermophilic bacterium Thermotoga neapolitana. Extremophiles 6:369-375.
19. Ivey, D. M., and T. A. Krulwich. 1991. Organization and nucleotide sequence of the atp genes encoding the ATP synthase from alkaliphilic Bacillus firmus OF4. Mol. Gen. Genet. 229:292-300.
20. o proposed to be involved in proton translocation through the ATP synthase. Res. Microbiol. 143:467-470.
21. + in the c subunit of the ATP synthase from Propionigenium modestum. Biochemistry 36:9185-9194.
22. o-ATP synthase from a thermoalkaliphilic Bacillus sp. strain TA2.A1. Biochim. Biophys. Acta 1676:112-117.
23. Keis, S., J. T. Sullivan, and D. T. Jones. 2001. Physical and genetic map of the Clostridium saccharobutylicum (formerly Clostridium acetobutylicum) NCP 262 chromosome. Microbiology 147:1909-1922.
24. o-ATPase of Propionigenium modestum from the reaction with dicyclohexylcarbodiimide. J. Biol. Chem. 268:14557-14560.
25. Knol, J., K. Sjollema, and B. Poolman. 1998. Detergent-mediated reconstitution of membrane proteins. Biochemistry 37:16410-16415.
26. Kobayashi, H., and Y. Anraku. 1972. Membrane-bound adenosine triphosphatase of Escherichia coli. J. Biochem. 71:387-399.
27. Krulwich, T. A. 1995. Alkaliphiles: 'basic' molecular problems of pH tolerance and bioenergetics. Mol. Microbiol. 15:403-410.
28. Krulwich, T. A., M. Ito, R. Gilmour, D. B. Hicks, and A. A. Guffanti. 1998. Energetics of alkaliphilic Bacillus species: physiology and molecules. Adv. Microb. Physiol. 40:401-438.
29. Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
30. Laubinger, W., and P. Dimroth. 1988. Characterization of the ATP synthase of Propionigenium modestum as a primary sodium pump. Biochemistry 27:7531-7537.
31. o type. Eur. J. Biochem. 168:475-480.
32. Laubinger, W., and P. Dimroth. 1989. The sodium ion translocating adenosine triphosphatase of Propionigenium modestum pumps protons at low sodium ion concentrations. Biochemistry 28:7194-7198.
33. Lerner, C. G., and M. Inouye. 1990. Low copy number plasmids for regulated low-level expression of cloned genes in Escherichia coli with blue/white insert screening capability. Nucleic Acids Res. 18:4631.
34. Li, Y., L. Mandelco, and J. Wiegel. 1993. Isolation and characterization of a moderately thermophilic anaerobic alkaliphile. Clostridium paradozum sp. nov. Int. J. Syst. Bacteriol. 43:450-460.
35. Linnett, P. E., and R. B. Beechey. 1979. Inhibitors of the ATP synthase system. Methods Enzymol. 55:472-518.
36. o-ATPase of Propionigenium modestum. Production, purification and properties of the protein in dodecylsulfate solution. Eur. J. Biochem. 247:820-825.
37. o ATP synthases. EMBO Rep. 3:1094-1098.
38. Meier, T., U. Matthey, C. von Ballmoos, J. Vonck, T. Krug von Nidda, W. Kühlbrandt, and P. Dimroth. 2003. Evidence for structural integrity in the undecameric c-rings isolated from sodium ATP synthases. J. Mol. Biol. 325:389-397.
39. +-ATPase from Hyobacter tartaricus. Science 308:659-662.
40. Nesterenko, M. V., M. Tilley, and S. J. Upton. 1994. A simple modification of Blum's silver stain method allows for 30 minute detection of proteins in polyacrylamide gels. J. Biochem. Biophys. Methods 28:239-242.
41. o ATPase of Hyobacter tartaricus, a sodium ion pump. J. Bacteriol. 180:3312-3316.
42. Ohta, S., M. Yohda, M. Ishizuka, H. Hirata, T. Hamamoto, Y. Otawara-Hamamoto, K. Matsuda, and Y. Kagawa. 1988. Sequence and over-expression of subunits of adenosine triphosphate synthase in thermophilic bacterium PS3. Biochim. Biophys. Acta 933:141-155.
43. Peddie, C. J., G. M. Cook, and H. W. Morgan. 1999. Sodium-dependent glutamate uptake by an alkaliphilic, thermophilic Bacillus strain, TA2.A1. J. Bacteriol. 181:3172-3177.
44. Prowe, S. G., J. L. C. M. van de Vossenberg, A. J. M. Driessen, G. Antranikian, and W. N. Konings. 1996. Sodium-coupled energy transduction in the newly isolated thermoalkaliphilic strain LBS3. J. Bacteriol. 178:4099-4104.
45. + specificity as revealed by sequence comparisons. FEBS Lett. 404:269-271.
46. o-type enzyme. Eur. J. Biochem. 223:275-283.
47. 1-ATPase single molecules. Nature 433:773-777.
48. o-ATP synthase. Biochim. Biophys. Acta 1553:188-211.
49. Speelmans, G., B. Poolman, T. Ahee, and W. N. Konings. 1993. Energy transduction in the thermophilic anaerobic bacterium Clostridium fervidus is exclusively coupled to sodium ions. Proc. Natl. Acad. Sci. USA 90:7975-7979.
50. Speelmans, G., B. Poolman, and W. N. Konings. 1993. Amino acid transport in the thermophilic anaerobe Clostridium fervidus is driven by an electrochemical sodium gradient. J. Bacteriol. 175:2060-2066.
51. o-ATPase from Acetobacterium woodii-probing the site(s) involved in ion-transport. Biochim. Biophys. Acta 1229:96-102.
52. Sturr, M. G., A. A. Guffanti, and T. A. Krulwich. 1994. Growth and bioenergetics of alkaliphilic Bacillus firmus OF4 in continuous culture at high pH. J. Bacteriol. 176:3111-3116.
53. van de Vossenberg, J. L. C. M., T. Ubbink-Kok, M. G. Elferink, A. J. M. Driessen, and W. N. Konings. 1995. Ion permeability of the cytoplasmic membrane limits the maximum growth temperature of bacteria and archaea. Mol. Microbiol. 18:925-932.
54. o ATP synthase. J. Biol. Chem. 277:3504-3510.
55. Walker, J. E., M. Saraste, M. J. Runswick, and N. J. Gay. 1982. Distantly related sequences in the α- and β-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold. EMBO J. 1:945-951.
56. Wang, Z., D. B. Hicks, A. A. Guffanti, K. Baldwin, and T. A. Krulwich. 2004. Replacement of amino acid sequence features of a- and c-subunits of ATP synthases of alkaliphilic Bacillus with the Bacillus consensus sequence results in defective oxidative phosphorylation and non-fermentative growth at pH 10.5. J. Biol. Chem. 279:26546-26554.
57. Wilkens, S., F. W. Dahlquist, L. P. McIntosh, L. W. Donaldson, and R. A. Capaldi. 1995. Structural features of the ε subunit of the Escherichia coli ATP synthase determined by NMR spectroscopy. Nat. Struct. Biol. 2:961-967.
58. Xie, D.-L., H. Lill, G. Hauska, M. Maeda, M. Futai, and N. Nelson. 1993. The atp2 operon of the green bacterium Chlorobium limicola. Biochim. Biophys. Acta 1172:267-273.
59. Yanisch-Perron, C., J. Vieira, and J. Messing. 1985. Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors. Gene 33:103-119.