The fully-active and structurally-stable form of the mitochondrial ATP synthase of Polytomella sp. is dimeric-Reference-Cited by-同舟云学术

The fully-active and structurally-stable form of the mitochondrial ATP synthase of Polytomella sp. is dimeric

Published:2009-02 Issue:1 Volume:41 Page:1-13
ISSN:0145-479X
Container-title:Journal of Bioenergetics and Biomembranes
language:en
Short-container-title:J Bioenerg Biomembr

Author:

Villavicencio-Queijeiro Alexa,Vázquez-Acevedo Miriam,Cano-Estrada Araceli,Zarco-Zavala Mariel,Tuena de Gómez Marietta,Mignaco Julio A.,Freire Monica M.,Scofano Helena M.,Foguel Debora,Cardol Pierre,Remacle Claire,González-Halphen Diego

Publisher

Springer Science and Business Media LLC

Subject

Cell Biology,Physiology

Link

http://link.springer.com/content/pdf/10.1007/s10863-009-9203-0.pdf

Reference46 articles.

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2. Arselin G, Vaillier J, Salin B, Schaeffer J, Giraud MF, Dautant A, Brèthes D, Velours J (2004) The modulation in subunits e and g amounts of yeast ATP synthase modifies mitochondrial cristae morphology. J Biol Chem 279:40392–40399

3. Atteia A, Dreyfus G, González-Halphen D (1997) Characterization of the alpha and beta-subunits of the F0F1-ATPase from the alga Polytomella spp., a colorless relative of Chlamydomonas reinhardtii. Biochim Biophys Acta 1320:275–284

4. Bornhövd C, Vogel F, Neupert W, Reichert AS (2006) Mitochondrial membrane potential is dependent on the oligomeric state of F1F0-ATP synthase supracomplexes. J Biol Chem 281:13990–13998

5. Brunner S, Everard-Gigot V, Stuart RA (2002) Su e of the yeast F1Fo-ATP synthase forms homodimers. J Biol Chem 277:48484–48489

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