The study of the pathogenic mechanism of mitochondrial diseases provides information on basic bioenergetics

Biochimica et Biophysica Acta - Bioenergetics

Volumn 1777, Issue 7-8, 2008, Pages 941-945

  Solaini, Giancarlo ^a   Harris, David A ^b   Lenaz, Giorgio ^a   Sgarbi, Gianluca ^a   Baracca, Alessandra ^a  

^a UNIVERSITY OF BOLOGNA   (Italy)

^b UNIVERSITY OF OXFORD   (United Kingdom)

Author keywords

ATP synthase; ATPase 6 subunit; Mitochondria; mtDNA mutation; Proton transport

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; ATPASE 6; OLIGOMYCIN; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE;

ARTICLE; BIOENERGY; CONTROLLED STUDY; DISORDERS OF MITOCHONDRIAL FUNCTIONS; HUMAN; HUMAN CELL; LYMPHOCYTE; MUTATION; NARP SYNDROME; PATHOGENESIS; PHENOTYPE; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTON TRANSPORT;

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; AMINO ACID SUBSTITUTION; ENERGY METABOLISM; HUMANS; KINETICS; LYMPHOCYTES; MITOCHONDRIA; MITOCHONDRIAL DISEASES; MODELS, MOLECULAR; PROTEIN CONFORMATION; PROTON-TRANSLOCATING ATPASES;

EID: 46349087708     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2008.04.034     Document Type: Article

References (37)

1. Walker J.E., and Dickson V.K. The peripheral stalk of the mitochondrial ATP synthase. Biochim. Biophys. Acta 1757 (2006) 286-296
2. Howitt S.M., Rodgers A.J., Hatch L.P., Gibson F., and Cox G.B. The coupling of the relative movement of the a and c subunits of the Fo to the conformational changes in the F1-ATPase. J. Bioenerg. Biomembranes. 28 (1996) 415-420
3. Rastogi V.K., and Girvin M.E. Structural changes linked to proton translocation by subunit c of the ATP synthase. Nature 402 (1999) 263-268
4. Vik S.B., Long J.C., Wada T., and Zhang D. A model for the structure of subunit a of the Escherichia coli ATP synthase and its role in proton translocation. Biochim. Biophys. Acta 1458 (2000) 457-466
5. 0-ATPase of Escherichia coli. Biochim. Biophys. Acta 1015 (1990) 264-268
6. Sgarbi G., Baracca A., Lenaz G., Valentino L.M., Carelli V., and Solaini G. Inefficient coupling between proton transport and ATP synthesis may be the pathogenic mechanism for NARP and Leigh syndrome resulting from the T8993G mutation in mtDNA. Biochem. J. 395 (2006) 493-500
7. 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
8. Aksimentiev A., Balabin I.A., Fillingame R.H., and Schulten K. Insights into the molecular mechanism of rotation in the Fo sector of ATP synthase. Biophys. J. 86 (2004) 1332-1344
9. +-ATPase from Ilyobacter tartaricus. Science 308 (2005) 659-662
10. Dimroth P., von Ballamoos C., and Meier T. Catalytic and mechanical cycles in F-ATP synthases. EMBO Rep. 7 (2006) 276-282
11. Vincent O.D., Schwem B.E., Steed P.R., Jiang W., and Fillingame R.H. Fluidity of structure and swivelling of helices in the subunit c ring of Escherichia coli ATP synthase as revealed by cysteine-cysteine cross-linking. J. Biol. Chem. 282 (2007) 33788-33794
12. Taylor R.W., and Turnbull D.M. Mitochondrial DNA mutations in human disease. Nature Rev. Genet. 6 (2005) 389-402
13. Lenaz G., Baracca A., Carelli V., D'Aurelio M., Sgarbi G., and Solaini G. Bioenergetics of mitochondrial diseases associated with mtDNA mutations. Biochim. Biophys. Acta-Bioenergetics. 1658 (2004) 89-94
14. Baracca A., Sgarbi G., Mattiazzi M., Casalena G., Pagnotta E., Valentino M.L., Moggio M., Lenaz G., Carelli V., and Solaini G. Biochemical phenotypes associated with the mitochondrial ATP6 gene mutations at nt8993. Biochim. Biophys. Acta Bioenerg 767 (2007) 913-919
15. 0-ATP synthase from Escherichia coli. A model for human mitochondrial disease. J Biol Chem. 268 (1993) 12250-12252
16. Ogilvie I., and Capaldi R.A. Mutations of the mitochondrially encoded ATPase 6 gene modelled in the ATP synthase of Escherichia coli. FEBS Lett. 453 (1999) 179-182
17. Solaini G., Sgarbi G., Lenaz G., and Baracca A. Evaluating mitochondrial membrane potential in cells. Biosci. Rep. 27 (2007) 11-21
18. Baracca A., Sgarbi G., Solaini G., and Lenaz G. Rhodamine 123 as a probe of mitochondrial membrane potential: evaluation of proton flux through Fo during ATP synthesis. Biochim. Biophys. Acta Bioenerg. 1606 (2003) 137-146
19. Lowry O.H., Rosenbrough N.J., Farr A.L., and Randall R.J. Protein measurement with the Folin phenol reagent. J. Biol. Chem. 193 (1951) 265-275
20. Lambert C., Leonard N., De Bolle X., and Depiereux E. ESyPred3D: prediction of proteins 3D structures. Bioinformatics 18 (2002) 1250-1256
21. Holt I.J., Harding A.E., Petty R.K., and Morgan-Hughes J.A. A new mitochondrial disease associated with mitochondrial DNA heteroplasmy. Am. J. Hum. Genet. 46, (1990) 428-433
22. Baracca A., Barogi S., Carelli V., Lenaz G., and Solaini G. Catalytic activities of mitochondrial ATP synthase in patients with mitochondrial DNA T8993G mutation in the ATPase 6 gene encoding subunit a. J. Biol. Chem. 275 (2000) 4177-4182
23. Garcia J.J., Ogilvie I., Robinson B.H., and Capaldi R. Structure, functioning, and assembly of the ATP synthase in cells from patients with the T8993G mitochondrial DNA mutation. Comparison with the enzyme in Rho(0) cells completely lacking mtDNA. J. Biol. Chem. 275 (2000) 11075-11081
24. 0-ATP synthase without preventing enzyme assembly and oligomerization. J. Biol. Chem. 282 (2007) 1051-1058
25. Vazquez-Memije M.E., Schanke S., Santorelli F.M., Kranz-Eble P., De Vivo D.C., and DiMauro S. Comparative biochemical studies of ATPases in cells from patients with the T8993G or T8993C mitochondrial DNA mutations. J. Inherit. Metab. Dis. 21 (1998) 829-836
26. Pallotti F., Baracca A., Hernandez-Rosa E., Walker W.F., Solaini G., Lenaz G., Melzi d'Eril G.V., DiMauro S., Schon E.A., and Davidson M. Biochemical analysis of respiratory function in cybrid cell lines harbouring mitochondrial DNA mutations. Biochem. J. 384, (2004) 287-293
27. Breen G.A., Miller D.L., Holmans P.L., and Welch G. Mitochondrial DNA of two independent oligomycin-resistant Chinese hamster ovary cell lines contains a single nucleotide change in the ATPase 6 gene. J. Biol. Chem. 261 (1986) 11680-11685
28. Ray M.K., Connerton I.F., and Griffiths D.E. DNA sequence analysis of the Olir2-76 and Ossr1-92 alleles of the Oli-2 region of the yeast Saccharomyces cerevisiae. Analysis of related amino-acid substitutions and protein-antibiotic interaction. Biochim. Biophys. Acta 951 (1988) 213-219
29. 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
30. Moore, K.J., Angevine, C.M., Owen, D.W., Schwem B.E., Fillingame, R.H., The cytoplasmic loops of subunit a of Escherichia coli ATP synthase may participate in the proton translocating mechanism J. Biol. Chem. 283 (2008) 13044-13052.
31. Devenish R.J., Prescott M., Boyle G.M., and Nagley P. The oligomycin axis of mitochondrial ATP synthase: OSCP and the proton channel. J. Bioenerg. Biomembranes 32, (2000) 507-514
32. Vik S.B., and Ishmukhametov R.R. Structure and function of subunit a of the ATP synthase of Escherichia coli. J. Bioenerg, Biomembranes 37, (2005) 445-449
33. Schon E.A., Santra S., Pallotti F., and Girvin M.E. Pathogenesis of primary defects in mitochondrial ATP synthesis. Semin. Cell Dev. Biol. 12 (2001) 441-448
34. Cain B.D., and Simoni R.D. Proton translocation by the F1F0ATPase of Escherichia coli. Mutagenic analysis of the a subunit. J. Biol. Chem. 264 (1989) 3292-3300
35. 0-ATP synthase. J. Biol. Chem. 283 (2008) 12365-12372.
36. Angevine C.M., Herold K.A.G., Vincent O.D., and Fillingame R.H. Aqueous access pathways in ATP synthase subunit a. J. Biol. Chem. 282, (2007) 9001-9007
37. Manfredi G., Gupta N., Vazquez-Memije M.E., Sadlock J.E., Spinazzola A., De Vivo D.C., and Schon E.A. Oligomycin induces a decrease in the cellular content of a pathogenic mutation in the human mitochondrial ATPase 6 gene. J. Biol. Chem. 274 (1999) 9386-9391