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.

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. Research Abstract Details 

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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. Abstract Text:

Miriam ,Pierre Cardol,Araceli Cano-Estrada,Marie Lapaille,Claire Remacle,Diego ,

Mitochondrial F(1)F( O )-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.

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. Publishing Authors By Initials

M ,P Cardol,A Cano-Estrada,M Lapaille,C Remacle,D ,

For similar algae: algae, green: volvox research abstracts see: algae: algae, green: volvox research

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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. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Journal of bioenergetics and biomembranes

VOLUME: 38

Page Numbers: 271-82

Journal Abbreviation: J. Bioenerg. Biomembr.

ISSN: 0145-479X

DAY: 3

MONTH: Dec

YEAR: 2006

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. Information

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LANGUAGE: eng

NlmUniqueID: 7701859

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. Keywords Mesh Terms:

KEYWORDS: Volvox

MESH TERMS: enzymology

Chemical & Substance for Abstract: 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. Information

Substance Name: Mitochondrial Proton-Translocating ATPas

Registry Number: EC 3.6.3.-

Grant and Affiliation Information for 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.

AFFILIATION: Departamento de Genética Molecular, Instituto de Fisiología Celular, Universidad Nacional Autónoma de México, Apartado Postal 70-600, Delegación Coyoacán, 04510, México D.F., Mexico.

Country: United States

AGENCY: United States FIC

GRANT: TW01176

ACRONYM: TW

MEDLINETA: J Bioenerg Biomembr

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