Oxa1 directly interacts with Atp9 and mediates its assembly into the mitochondrial F1Fo-ATP synthase complex.

Oxa1 directly interacts with Atp9 and mediates its assembly into the mitochondrial F1Fo-ATP synthase complex. Research Abstract Details 

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Oxa1 directly interacts with Atp9 and mediates its assembly into the mitochondrial F1Fo-ATP synthase complex. Abstract Text:

Lixia Jia,Mary K Dienhart,Rosemary A Stuart,

The yeast Oxa1 protein is involved in the biogenesis of the mitochondrial oxidative phosphorylation (OXPHOS) machinery. The involvement of Oxa1 in the assembly of the cytochrome oxidase (COX) complex, where it facilitates the cotranslational membrane insertion of mitochondrially encoded COX subunits, is well documented. In this study we have addressed the role of Oxa1, and its sequence-related protein Cox18/Oxa2, in the biogenesis of the F(1)F(o)-ATP synthase complex. We demonstrate that Oxa1, but not Cox18/Oxa2, directly supports the assembly of the membrane embedded F(o)-sector of the ATP synthase. Oxa1 was found to physically interact with newly synthesized mitochondrially encoded Atp9 protein in a posttranslational manner and in a manner that is not dependent on the C-terminal, matrix-localized region of Oxa1. The stable manner of the Atp9-Oxa1 interaction is in contrast to the cotranslational and transient interaction previously observed for the mitochondrially encoded COX subunits with Oxa1. In the absence of Oxa1, Atp9 was observed to assemble into an oligomeric complex containing F(1)-subunits, but its further assembly with subunit 6 (Atp6) of the F(o)-sector was perturbed. We propose that by directly interacting with newly synthesized Atp9 in a posttranslational manner, Oxa1 is required to maintain the assembly competence of the Atp9-F(1)-subcomplex for its association with Atp6.

Oxa1 directly interacts with Atp9 and mediates its assembly into the mitochondrial F1Fo-ATP synthase complex. Publishing Authors By Initials

L Jia,MK Dienhart,RA Stuart,

For similar proteins: fungal proteins: saccharomyces cerevisiae proteins research abstracts see: proteins: fungal proteins: saccharomyces cerevisiae proteins research

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Oxa1 directly interacts with Atp9 and mediates its assembly into the mitochondrial F1Fo-ATP synthase complex. Journal Published:

PUBLICATION TYPE: Research Support, U.S. Gov't,

Journal: Molecular biology of the cell

VOLUME: 18

Page Numbers: 1897-908

Journal Abbreviation:

ISSN: 1059-1524

DAY: 7

MONTH: 03

YEAR: 2007

Oxa1 directly interacts with Atp9 and mediates its assembly into the mitochondrial F1Fo-ATP synthase complex. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 9201390

Oxa1 directly interacts with Atp9 and mediates its assembly into the mitochondrial F1Fo-ATP synthase complex. Keywords Mesh Terms:

KEYWORDS: Saccharomyces cerevisiae Proteins

MESH TERMS: metabolism

Chemical & Substance for Abstract: Oxa1 directly interacts with Atp9 and mediates its assembly into the mitochondrial F1Fo-ATP synthase complex. Information

Substance Name: Mitochondrial Proton-Translocating ATPas

Registry Number: EC 3.6.3.-

Grant and Affiliation Information for Oxa1 directly interacts with Atp9 and mediates its assembly into the mitochondrial F1Fo-ATP synthase complex.

AFFILIATION: Department of Biological Sciences, Marquette University, Milwaukee, WI 53233, USA.

Country: United States

AGENCY: United States NIGMS

GRANT: R01GM61573

ACRONYM: GM

MEDLINETA: Mol Biol Cell

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