Evidence for the association of yeast mitochondrial ribosomes with Cox11p, a protein required for the CuB site formation of cytochrome c oxidase

Oleh Khalimonchuk, Kai Ostermann, Gerhard Rödel

Research output: Contribution to journalArticle

44 Citations (Scopus)

Abstract

Cytochrome c oxidase is the terminal enzyme of the mitochondrial (mt) respiratory chain. It contains copper ions, which are organized in two centres, CuA and CuB. The CuA site of subunit Cox2p is exposed to the mt intermembrane space, while the CuB site of subunit Cox1p is buried in the inner mt membrane. Incorporation of copper into the two centres is crucial for the assembly and activity of the enzyme. Formation of the CuB site is dependent on Cox11p, a copper-binding protein of the mt inner membrane. Here, we experimentally prove that Cox11p possesses a Nin-Cout topology, with the C-terminal copper-binding domain exposed in the mt intermembrane space. Furthermore, we provide evidence for the association of Cox11p with the mt translation machinery. We propose a model in which the CuB site is co-translationally formed by a transient interaction between Cox11p and the nascent Cox1p in the intermembrane space.

Original languageEnglish (US)
Pages (from-to)223-233
Number of pages11
JournalCurrent Genetics
Volume47
Issue number4
DOIs
StatePublished - Apr 1 2005

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Electron Transport Complex IV
Copper
Yeasts
Mitochondrial Membranes
Proteins
Enzymes
Electron Transport
Ions
Mitochondrial Ribosomes

Keywords

  • Copper metabolism
  • Cox11p
  • Cytochrome c oxidase
  • Mitochondria
  • Mitoribosomes
  • Saccharomyces cerevisiae

ASJC Scopus subject areas

  • Genetics

Cite this

Evidence for the association of yeast mitochondrial ribosomes with Cox11p, a protein required for the CuB site formation of cytochrome c oxidase. / Khalimonchuk, Oleh; Ostermann, Kai; Rödel, Gerhard.

In: Current Genetics, Vol. 47, No. 4, 01.04.2005, p. 223-233.

Research output: Contribution to journalArticle

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N2 - Cytochrome c oxidase is the terminal enzyme of the mitochondrial (mt) respiratory chain. It contains copper ions, which are organized in two centres, CuA and CuB. The CuA site of subunit Cox2p is exposed to the mt intermembrane space, while the CuB site of subunit Cox1p is buried in the inner mt membrane. Incorporation of copper into the two centres is crucial for the assembly and activity of the enzyme. Formation of the CuB site is dependent on Cox11p, a copper-binding protein of the mt inner membrane. Here, we experimentally prove that Cox11p possesses a Nin-Cout topology, with the C-terminal copper-binding domain exposed in the mt intermembrane space. Furthermore, we provide evidence for the association of Cox11p with the mt translation machinery. We propose a model in which the CuB site is co-translationally formed by a transient interaction between Cox11p and the nascent Cox1p in the intermembrane space.

AB - Cytochrome c oxidase is the terminal enzyme of the mitochondrial (mt) respiratory chain. It contains copper ions, which are organized in two centres, CuA and CuB. The CuA site of subunit Cox2p is exposed to the mt intermembrane space, while the CuB site of subunit Cox1p is buried in the inner mt membrane. Incorporation of copper into the two centres is crucial for the assembly and activity of the enzyme. Formation of the CuB site is dependent on Cox11p, a copper-binding protein of the mt inner membrane. Here, we experimentally prove that Cox11p possesses a Nin-Cout topology, with the C-terminal copper-binding domain exposed in the mt intermembrane space. Furthermore, we provide evidence for the association of Cox11p with the mt translation machinery. We propose a model in which the CuB site is co-translationally formed by a transient interaction between Cox11p and the nascent Cox1p in the intermembrane space.

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