An Expanded and Flexible Form of the Vacuolar ATPase Membrane Sector

Structure

Volumn 14, Issue 7, 2006, Pages 1149-1156

  Clare, Daniel K ^a   Orlova, Elena V ^a   Finbow, Malcolm A ^b   Harrison, Michael A ^c   Findlay, John B C ^c   Saibil, Helen R ^a  

^a UNIVERSITY OF LONDON   (United Kingdom)

^b GLASGOW CALEDONIAN UNIVERSITY   (United Kingdom)

^c UNIVERSITY OF LEEDS   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE;

ARTICLE; CRYOELECTRON MICROSCOPY; CRYSTAL STRUCTURE; ENZYME CONFORMATION; ENZYME MECHANISM; ENZYME STRUCTURE; ENZYME SUBUNIT; IMAGE PROCESSING; LOBSTER; MEMBRANE FUSION; MEMBRANE STRUCTURE; NEPHROPS NORVEGICUS; PRIORITY JOURNAL; STRUCTURE ANALYSIS;

AMINO ACID SEQUENCE; ANIMALS; CELL MEMBRANE; CRYOELECTRON MICROSCOPY; CRYSTALLOGRAPHY; MOLECULAR SEQUENCE DATA; NEPHROPIDAE; PROTEIN CONFORMATION; PROTEIN SUBUNITS; VACUOLAR PROTON-TRANSLOCATING ATPASES;

NEPHROPS NORVEGICUS;

EID: 33745867962     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.str.2006.05.014     Document Type: Article

References (58)

1. Arai H., Berne M., Terres G., Terres H., Puopolo K., and Forgac M. Subunit composition and ATP site labeling of the coated vesicle proton-translocating adenosinetriphosphatase. Biochemistry 26 (1987) 6632-6638
2. Arai H., Terres G., Pink S., and Forgac M. Topography and subunit stoichiometry of the coated vesicle proton pump. J. Biol. Chem. 263 (1988) 8796-8802
3. 2+-releasing channel. J. Cell Biol. 162 (2003) 211-222
4. +-ATPase/synthase by electron microscopy. Structure 12 (2004) 1789-1798
5. Bowman E.J., Tenney K., and Bowman B.J. Isolation of genes encoding the Neurospora vacuolar ATPase. Analysis of Vma-1 encoding the 67-kDa subunit reveals homology to other ATPases. J. Biol. Chem. 263 (1988) 13994-14001
6. Bowman B.J., Allen R., Wechser M.A., and Bowman E.J. Isolation of genes encoding the Neurospora vacuolar ATPase. Analysis of Vma-2 encoding the 57-kDa polypeptide and comparison to Vma-1. J. Biol. Chem. 263 (1988) 14002-14007
7. Crowther R.A., Henderson R., and Smith J.M. MRC image processing suite. J. Struct. Biol. 116 (1996) 9-16
8. 1-ATP synthase. Nat. Struct. Mol. Biol. 11 (2004) 135-141
9. Elston T., Wang H., and Oster G. Energy transduction in ATP synthase. Nature 391 (1998) 510-513
10. Fethiere J., Venzke D., Diepholz M., Seybert A., Geerlof A., Gentzel M., Wilm M., and Bottcher B. Building the stator of the yeast vacuolar-ATPase: specific interaction between subunits E and G. J. Biol. Chem. 279 (2004) 40670-40676
11. Fillingame R.H. Molecular rotary motors. Science 286 (1999) 1687-1688
12. Finbow M.E., Eldridge T., Buultjens J., Lane N.J., Shuttleworth J., and Pitts J.D. Isolation and characterisation of arthropod gap junctions. EMBO J. 3 (1984) 2271-2278
13. +-ATPase. Protein Eng. 5 (1992) 7-15
14. Fleishman S.J., Unger V.M., Yeager M., and Ben-Tal N. A C-alpha model for the transmembrane α helices of gap junction intercellular channels. Mol. Cell 15 (2004) 879-888
15. Frank J., Radermacher M., Penczek P., Zhu J., Li Y., Ladjadj M., and Leith A. SPIDER and WEB: processing and visualization of images in 3D electron microscopy and related Fields. J. Struct. Biol. 116 (1996) 190-199
16. o sector of the V-ATPase, synaptobrevin, and synaptophysin are associated on synaptic vesicles in a triton X-100-resistant, freeze-thawing sensitive, complex. J. Biol. Chem. 271 (1996) 2193-2198
17. Girvin M.E., Rastogi V.K., Abildgaard F., Markley J.L., and Fillingame R.H. Solution structure of the transmembrane H+-transporting subunit c of the F1F0 ATP synthase. Biochemistry 25 (1998) 8817-8824
18. Gruber G., Godovac-Zimmermann J., Link T.A., Coskun U., Rizzo V.F., Betz C., and Bailer S.M. Expression, purification, and characterisation of subunit E, an essential subunit of the vacuolar ATPase. Biochem. Biophys. Res. Commun. 298 (2002) 383-391
19. +-ATPase: site-directed labeling with N-(1-pyrenyl)cyclohexylcarbodiimide and fluorescence quenching analysis. Biochemistry 39 (2000) 7531-7537
20. Henderson R., Baldwin J.M., Downing K.H., Lepault J., and Zemlin F. Structure of purple membrane from Halobacterium halobium: recording, measurement and evaluation of electron micrographs at 3.5 Å resolution. Ultramicroscopy 19 (1986) 147-178
21. o subunit a1 is required for a late step in synaptic vesicle exocytosis in Drosophila. Cell 121 (2005) 607-620
22. +-ATPase. J. Biol. Chem. 272 (1997) 4795-4803
23. Holzenburg A., Jones P.C., Franklin T., Pali T., Heimburg T., Marsh D., Findlay J.B.C., and Finbow M.E. Evidence for a common structure for a class of membrane channels. Eur. J. Biochem. 13 (1993) 21-30
24. Jiang W., Hermolin J., and Fillingame R.H. The preferred stoichiometry of c subunits in the rotary motor sector of Escherichia coli ATP synthase is 10. Proc. Natl. Acad. Sci. USA 98 (2001) 4966-4971
25. John S.A., Saner D., Pitts J.D., Holzenburg A., Finbow M.E., and Lal R. Atomic force microscopy of arthropod gap junctions. J. Struct. Biol. 120 (1997) 22-31
26. Jones T.A., Zou J.-Y., Cowan S.W., and Kjeldgaard M. Improved methods for the building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47 (1991) 110-119
27. +-ATPase subunit F (Vma7p). Mol. Membr. Biol. 18 (2001) 283-290
28. 1-ATPase. FEBS Lett. 504 (2001) 152-160
29. Kane P.M. Regulation of V-ATPases by reversible disassembly. FEBS Lett. 469 (2000) 137-141
30. Meier T., Matthey U., Henzen F., Dimroth P., and Muller D.J. The central plug in the reconstituted undecameric c cylinder of a bacterial ATP synthase consists of phospholipids. FEBS Lett. 505 (2001) 353-356
31. Meier T., Matthey U., von Ballmoos C., Vonck J., Krug von Nidda T., Kuhlbrandt W., and Dimroth P. Evidence for structural integrity in the undecameric c-rings isolated from sodium ATP synthases. J. Mol. Biol. 325 (2003) 389-397
32. +/ATP ratio and permissive elastic coupling. Proc. Natl. Acad. Sci. USA 101 (2004) 12159-12164
33. Muller V. An exceptional variability in the motor of archaeal A(1)A(0) ATPases: from multimeric to monomeric rotors comprising 6-13 ion binding sites. J. Bioenerg. Biomembr. 36 (2004) 115-125
34. Muller V., and Gruber G. ATP synthases: structure, function and evolution of unique energy converters. Cell. Mol. Life Sci. 60 (2003) 474-494
35. +-motive V-ATPase from Enterococcus hirae contains a heptameric rotor. J. Biol. Chem. 278 (2003) 21162-21167
36. +-ATPase from Enterococcus hirae. Science 308 (2005) 654-659
37. +-ATPases. Trends Biochem. Sci. 3 (1989) 113-116
38. +)-ATPases-nature's most versatile proton pumps. Nat. Rev. Mol. Cell Biol. 3 (2002) 94-103
39. Oster G., and Wang H. Reverse engineering a protein: the mechanochemistry of ATP synthase. Biochim. Biophys. Acta 1458 (2000) 482-510
40. Pali T., Finbow M.E., Holzenburg A., Findlay J.B.C., and Marsh D. Lipid-protein interactions and assembly of the 16-kDa channel polypeptide from Nephrops norvegicus. Studies with spin-label electron spin resonance spectroscopy and electron microscopy. Biochemistry 34 (1995) 9211-9218
41. Peters C., Bayer M.J., Buhler S., Andersen J.S., Mann M., and Mayer A. Trans-complex formation by proteolipid channels in the terminal phase of membrane fusion. Nature 409 (2001) 581-588
42. 0 symmetry mismatch is not obligatory. EMBO Rep. 6 (2005) 1040-1044
43. +-ATPase proton pore. J. Biol. Chem. 275 (2000) 23654-23660
44. 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
45. Rubinstein J.L., Walker J.E., and Henderson R. Structure of the mitochondrial ATP synthase by electron cryomicroscopy. EMBO J. 22 (2003) 6182-6192
46. 1): direct observation. Science 286 (1999) 1722-1724
47. Seelert H., Poetsch A., Dencher N.A., Engel A., Stahlberg H., and Muller D.J. Structural biology. Proton-powered turbine of a plant motor. Nature 405 (2000) 418-419
48. Sikerwar S.S., Downing K.H., and Glaeser R.M. Three-dimensional structure of an invertebrate intercellular communicating junction. J. Struct. Biol. 106 (1991) 255-263
49. Stock D., Leslie A.G., and Walker J.E. Molecular architecture of the rotary motor in ATP synthase. Science 286 (1999) 1700-1705
50. +-ATPase. Annu. Rev. Cell Dev. Biol. 13 (1997) 779-808
51. +-ATPase from chromaffin granules. J. Biol. Chem. 269 (1994) 24102-24106
52. +-ATPase of thermophilic bacterium Caloramator fervidus. J. Mol. Biol. 296 (2000) 311-321
53. Unger V.M., Kumar N.M., Gilula N.B., and Yeager M. Three-dimensional structure of a recombinant gap junction membrane channel. Science 283 (1999) 1176-1180
54. van Heel M., Harauz G., Orlova E.V., Schmidt R., and Schatz M. A new generation of the IMAGIC image processing system. J. Struct. Biol. 116 (1996) 17-24
55. Venzke D., Domgall I., Kocher T., Fethiere J., Fischer S., and Bottcher B. Elucidation of the stator organization in the V-ATPase of Neurospora crassa. J. Mol. Biol. 349 (2005) 659-669
56. Wilkens S., and Forgac M. Three-dimensional structure of the vacuolar ATPase proton channel by electron microscopy. J. Biol. Chem. 276 (2001) 44064-44068
57. Wilkens S., Vasilyeva E., and Forgac M. Structure of the vacuolar ATPase by electron microscopy. J. Biol. Chem. 274 (1999) 31804-31810
58. Yokoyama K., Nakano M., Imamura H., Yoshida M., and Tamakoshi M. Rotation of the proteolipid ring in the V-ATPase. J. Biol. Chem. 278 (2003) 24255-24258