Literature DB >> 11576527

The central plug in the reconstituted undecameric c cylinder of a bacterial ATP synthase consists of phospholipids.

T Meier1, U Matthey, F Henzen, P Dimroth, D J Müller.   

Abstract

The isolated rotor cylinder of the ATP synthase from Ilyobacter tartaricus was reconstituted into two-dimensional crystalline arrays. Atomic force microscopy imaging indicated a central cavity on one side of the rotor and a central plug protruding from the other side. Upon incubation with phospholipase C, the plug disappeared, but the appearance of the surrounding c subunit oligomer was not affected. This indicates that the plug consists of phospholipids. As the detergent-purified c cylinder is completely devoid of phospholipids, these are incorporated into the central hole from one side of the cylinder during the reconstitution procedure.

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Year:  2001        PMID： 11576527     DOI： 10.1016/s0014-5793(01)02837-x

Source DB:  PubMed          Journal:  FEBS Lett        ISSN： 0014-5793            Impact factor:   4.124


  32 in total

1.  Subnanometre-resolution structure of the intact Thermus thermophilus H+-driven ATP synthase.

Authors:  Wilson C Y Lau; John L Rubinstein
Journal:  Nature       Date:  2011-12-18       Impact factor: 49.962

2.  Engineering rotor ring stoichiometries in the ATP synthase.

Authors:  Denys Pogoryelov; Adriana L Klyszejko; Ganna O Krasnoselska; Eva-Maria Heller; Vanessa Leone; Julian D Langer; Janet Vonck; Daniel J Müller; José D Faraldo-Gómez; Thomas Meier
Journal:  Proc Natl Acad Sci U S A       Date:  2012-05-24       Impact factor: 11.205

3.  Structural study on the architecture of the bacterial ATP synthase Fo motor.

Authors:  Jonna K Hakulinen; Adriana L Klyszejko; Jan Hoffmann; Luise Eckhardt-Strelau; Bernd Brutschy; Janet Vonck; Thomas Meier
Journal:  Proc Natl Acad Sci U S A       Date:  2012-06-26       Impact factor: 11.205

4.  Microscopic rotary mechanism of ion translocation in the F(o) complex of ATP synthases.

Authors:  Denys Pogoryelov; Alexander Krah; Julian D Langer; Özkan Yildiz; José D Faraldo-Gómez; Thomas Meier
Journal:  Nat Chem Biol       Date:  2010-10-24       Impact factor: 15.040

5.  Structure of intact Thermus thermophilus V-ATPase by cryo-EM reveals organization of the membrane-bound V(O) motor.

Authors:  Wilson C Y Lau; John L Rubinstein
Journal:  Proc Natl Acad Sci U S A       Date:  2010-01-06       Impact factor: 11.205

6.  High-resolution structure of the rotor ring of a proton-dependent ATP synthase.

Authors:  Denys Pogoryelov; Ozkan Yildiz; José D Faraldo-Gómez; Thomas Meier
Journal:  Nat Struct Mol Biol       Date:  2009-09-27       Impact factor: 15.369

7.  The c15 ring of the Spirulina platensis F-ATP synthase: F1/F0 symmetry mismatch is not obligatory.

Authors:  Denys Pogoryelov; Jinshu Yu; Thomas Meier; Janet Vonck; Peter Dimroth; Daniel J Muller
Journal:  EMBO Rep       Date:  2005-11       Impact factor: 8.807

Review 8.  ATP synthase c-subunit ring as the channel of mitochondrial permeability transition: Regulator of metabolism in development and degeneration.

Authors:  Nelli Mnatsakanyan; Elizabeth Ann Jonas
Journal:  J Mol Cell Cardiol       Date:  2020-05-24       Impact factor: 5.000

9.  The c-ring stoichiometry of ATP synthase is adapted to cell physiological requirements of alkaliphilic Bacillus pseudofirmus OF4.

Authors:  Laura Preiss; Adriana L Klyszejko; David B Hicks; Jun Liu; Oliver J Fackelmayer; Özkan Yildiz; Terry A Krulwich; Thomas Meier
Journal:  Proc Natl Acad Sci U S A       Date:  2013-04-23       Impact factor: 11.205

10.  A new type of proton coordination in an F(1)F(o)-ATP synthase rotor ring.

Authors:  Laura Preiss; Ozkan Yildiz; David B Hicks; Terry A Krulwich; Thomas Meier
Journal:  PLoS Biol       Date:  2010-08-03       Impact factor: 8.029
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