Modular assembly of yeast mitochondrial ATP synthase and cytochrome oxidase

The respiratory pathway of mitochondria is composed of four electron transfer complexes and the ATP synthase. In this article, we review evidence from studies of Saccharomyces cerevisiae that both ATP synthase and cytochrome oxidase (COX) are assembled from independent modules that correspond to structurally and functionally identifiable components of each complex. Biogenesis of the respiratory chain requires a coordinate and balanced expression of gene products that become partner subunits of the same complex, but are encoded in the two physically separated genomes. Current evidence indicates that synthesis of two key mitochondrial encoded subunits of ATP synthase is regulated by the F1 module. Expression of COX1 that codes for a subunit of the COX catalytic core is also regulated by a mechanism that restricts synthesis of this subunit to the availability of a nuclear-encoded translational activator. The respiratory chain must maintain a fixed stoichiometry of the component enzyme complexes during cell growth. We propose that high-molecular-weight complexes composed of Cox6, a subunit of COX, and of the Atp9 subunit of ATP synthase play a key role in establishing the ratio of the two complexes during their assembly.

Medienart:

E-Artikel

Erscheinungsjahr:

2020

Erschienen:

2020

Enthalten in:

Zur Gesamtaufnahme - volume:401

Enthalten in:

Biological chemistry - 401(2020), 6-7 vom: 26. Mai, Seite 835-853

Sprache:

Englisch

Beteiligte Personen:

Franco, Leticia Veloso Ribeiro [VerfasserIn]
Su, Chen Hsien [VerfasserIn]
Tzagoloff, Alexander [VerfasserIn]

Links:

Volltext

Themen:

ATP synthase
Atp9
Cox6
Cytochrome oxidase
EC 1.9.3.1
EC 3.6.3.-
Electron Transport Complex IV
Journal Article
Mitochondrial Proton-Translocating ATPases
Mitochondrial biogenesis
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Review
Saccharomyces cerevisiae
Saccharomyces cerevisiae Proteins

Anmerkungen:

Date Completed 14.06.2021

Date Revised 14.06.2021

published: Print

Citation Status MEDLINE

doi:

10.1515/hsz-2020-0112

funding:

Förderinstitution / Projekttitel:

PPN (Katalog-ID):

NLM307308898