Direct observation of proton pumping by a eukaryotic P-type ATPase

Science

Volumn 351, Issue 6280, 2016, Pages 1469-1473

  Veshaguri, Salome ^a   Christensen, Sune M ^a,d   Kemmer, Gerdi C ^a   Ghale, Garima ^a   Møller, Mads P ^a   Lohr, Christina ^a   Christensen, Andreas L ^a   Justesen, Bo H ^a   Jørgensen, Ida L ^a   Schiller, Jürgen ^b   Hatzakis, Nikos S ^a   Grabe, Michael ^c   Günther Pomorski, Thomas ^a   Stamou, Dimitrios ^a  

^a UNIVERSITY OF COPENHAGEN   (Denmark)

^b UNIVERSITY OF LEIPZIG   (Germany)

^c UNIVERSITY OF CALIFORNIA   (United States)

^d NOVOZYMES A S   (Denmark)

Author keywords

[No Author keywords available]

Indexed keywords

PROTON TRANSPORTING ADENOSINE TRIPHOSPHATASE; AHA2 PROTEIN, ARABIDOPSIS; ARABIDOPSIS PROTEIN; PROTON; VALINOMYCIN;

BIOCHEMISTRY; CELLS AND CELL COMPONENTS; ENZYME ACTIVITY; EUKARYOTE; HERB; INHIBITION; MEMBRANE; MOLECULAR ANALYSIS; PH;

ACIDIFICATION; ALLOSTERISM; ARABIDOPSIS THALIANA; ARTICLE; BLEACHING; CONTROLLED STUDY; ENZYME ACTIVITY; FLUORESCENCE; LIPID VESICLE; MEMBRANE POTENTIAL; MOLECULAR DYNAMICS; NONHUMAN; PERMEABILITY; PH; PRIORITY JOURNAL; PROTON TRANSPORT; STOICHIOMETRY; ANTAGONISTS AND INHIBITORS; CHEMISTRY; DRUG EFFECTS; ION TRANSPORT; METABOLISM; MOLECULAR IMAGING; PHYSIOLOGY; PROTEIN TERTIARY STRUCTURE;

ARABIDOPSIS THALIANA; EUKARYOTA;

ALLOSTERIC REGULATION; ARABIDOPSIS PROTEINS; HYDROGEN-ION CONCENTRATION; ION TRANSPORT; MEMBRANE POTENTIALS; MOLECULAR IMAGING; PROTEIN STRUCTURE, TERTIARY; PROTON-TRANSLOCATING ATPASES; PROTONS; VALINOMYCIN;

EID: 84962256385     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.aad6429     Document Type: Article

References (29)

1. F. Ashcroft, D. Gadsby, C. Miller, Philos. Trans. R. Soc. London Ser. B 364, 145-147 (2009).
2. E. Neher, B. Sakmann, Nature 260, 799-802 (1976).
3. J. P. Morth et al., Nat. Rev. Mol. Cell Biol. 12, 60-70 (2011).
4. L. J. DeFelice, T. Goswami, Annu. Rev. Physiol. 69, 87-112 (2007).
5. R. Peters, Annu. Rev. Biophys. Biomol. Struct. 32, 47-67 (2003).
6. A. Tonnesen, S. M. Christensen, V. Tkach, D. Stamou, Biophys. J. 106, 201-209 (2014).
7. R. Watanabe et al., Nat. Commun. 5, 4519 (2014).
8. M. Li et al., J. Am. Chem. Soc. 137, 16055-16063 (2015).
9. B. P. Pedersen, M. J. Buch-Pedersen, J. P. Morth, M. G. Palmgren, P. Nissen, Nature 450, 1111-1114 (2007).
10. M. G. Palmgren, C. Larsson, M. Sommarin, J. Biol. Chem. 265, 13423-13426 (1990).
11. M. G. Palmgren, P. Nissen, Annu. Rev. Biophys. 40, 243-266 (2011).
12. See materials and methods and supplementary information on Science Online
13. S. Mathiasen et al., Nat. Methods 11, 931-934 (2014).
14. P. M. Bendix, M. S. Pedersen, D. Stamou, Proc. Natl. Acad. Sci. U.S.A. 106, 12341-12346 (2009).
15. D. Stamou, C. Duschl, E. Delamarche, H. Vogel, Angew. Chem. Int. Ed. Engl. 42, 5580-5583 (2003).
16. G. C. Kemmer et al., Analyst 140, 6313-6320 (2015).
17. L. Iversen et al., Science 345, 50-54 (2014).
18. M. J. Comstock et al., Science 348, 352-354 (2015).
19. T. Yanagida, Y. Ishii, Eds., Single Molecule Dynamics in Life Science (Wiley-VCH, Weinheim, Germany, 2009).
20. X. S. Xie, in Single Molecule Spectroscopy in Chemistry, Physics and Biology, A. Graslund, R. Rigler, J. Widengren, Eds. (Springer-Verlag Berlin, 2010), vol. 96, pp. 435-448.
21. N. Akyuz et al., Nature 518, 68 (2015).
22. C. E. Aitken, J. D. Puglisi, Nat. Struct. Mol. Biol. 17, 793-800 (2010).
23. G.-W. Li, E. Oh, J. S. Weissman, Nature 484, 538-541 (2012).
24. A. R. Subramaniam, B. M. Zid, E. K. O'Shea, Cell 159, 1200-1211 (2014).
25. B. Sakmann, E. Neher, Eds., Single-Channel Recording (Springer, New York, ed. 2, 2009).
26. M. Grabe, G. Oster, J. Gen. Physiol. 117, 329-344 (2001).
27. M. C. Berman, Biochim. Biophys. Acta 1513, 95-121 (2001).
28. N. Nelson, A. Sacher, H. Nelson, Nat. Rev. Mol. Cell Biol. 3, 876-881 (2002).
29. M. G. Palmgren, M. Sommarin, R. Serrano, C. Larsson, J. Biol. Chem. 266, 20470-20475 (1991).