Reference : The mitochondrial ATP synthase of chlorophycean algae contains eight subunits of unknown...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/40729
The mitochondrial ATP synthase of chlorophycean algae contains eight subunits of unknown origin involved in the formation of an atypical stator-stalk and in the dimerization of the complex
English
Vazquez-Acevedo, Miriam [> > > >]
Cardol, Pierre mailto [Université de Liège - ULg > Département des sciences de la vie > Génétique >]
Cano-Estrada, Araceli [> > > >]
Lapaille, Marie mailto [Université de Liège - ULg > Département des sciences de la vie > Génétique >]
Remacle, Claire mailto [Université de Liège - ULg > Département des sciences de la vie > Génétique >]
Gonzalez-Halphen, Diego [> > > >]
2006
Journal of Bioenergetics & Biomembranes
Kluwer Academic/Plenum Publishers
38
5-6
271-282
Yes (verified by ORBi)
International
0145-479X
New York
NY
[en] Mitochondrial F1FO-ATP synthase of Chlamydomonas reinhardtii and Polytomella sp. is a dimer of 1,600,000 Da. In Chlamydomonas the enzyme lacks the classical subunits that constitute the peripheral stator-stalk as well as those involved in the dimerization of the fungal and mammal complex. Instead, it contains eight novel polypeptides named ASA1 to 8. We show that homologs of these subunits are also present in the chlorophycean algae Polytomella sp. and Volvox carterii. Blue Native Gel Electrophoresis analysis of mitochondria from different green algal species also indicates that stable dimeric mitochondrial ATP synthases may be characteristic of all Chlorophyceae. One additional subunit, ASA9, was identified in the purified mitochondrial ATP synthase of Polytomella sp. The dissociation profile of the Polytomella enzyme at high-temperatures and cross-linking experiments finally suggest that some of the ASA polypeptides constitute a stator-stalk with a unique architecture, while others may be involved in the formation of a highly-stable dimeric complex. The algal enzyme seems to have modified the structural features of its surrounding scaffold, while conserving almost intact the structure of its catalytic subunits.
http://hdl.handle.net/2268/40729
also: http://hdl.handle.net/2268/35892
10.1007/s10863-006-9046-x

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