English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  COA6 facilitates cytochrome c oxidase biogenesis as thiol-reductase for copper metallochaperones in mitochondria.

Pacheu-Grau, D., Wasilewski, M., Oeljeklaus, S., Gibhardt, C. S., Aich, A., Chudenkova, M., et al. (2020). COA6 facilitates cytochrome c oxidase biogenesis as thiol-reductase for copper metallochaperones in mitochondria. Journal of Molecular Biology, (in press). doi:10.1016/j.jmb.2020.01.036.

Item is

Basic

show hide
Item Permalink: http://hdl.handle.net/21.11116/0000-0005-B6AE-A Version Permalink: http://hdl.handle.net/21.11116/0000-0005-B6B1-5
Genre: Journal Article

Files

show Files
hide Files
:
3195119.pdf (Preprint), 15MB
Name:
3195119.pdf
Description:
-
Visibility:
Public
MIME-Type / Checksum:
application/pdf / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Locators

show

Creators

show
hide
 Creators:
Pacheu-Grau, D., Author
Wasilewski, M., Author
Oeljeklaus, S., Author
Gibhardt, C. S., Author
Aich, A., Author
Chudenkova, M., Author
Dennerlein, S., Author
Deckers, M., Author
Bogeski, I., Author
Warscheid, B., Author
Chacinska, A., Author
Rehling, P.1, Author              
Affiliations:
1Max Planck Fellow Peter Rehling, ou_1298545              

Content

show
hide
Free keywords: COA6; Cu(A) center; copper metallochaperones; cytochrome c oxidase; mitochondria
 Abstract: The mitochondrial cytochrome c oxidase, the terminal enzyme of the respiratory chain, contains heme and copper centers for electron transfer. The conserved COX2 subunit contains the CuA site, a binuclear copper center. The copper chaperones SCO1, SCO2, and COA6 are required for CuA center formation. Loss of function of these chaperones and the concomitant cytochrome c oxidase deficiency cause severe human disorders. Here we analyzed the molecular function of COA6 and the consequences of COA6 deficiency for mitochondria. Our analyses show that loss of COA6 causes combined complex I and complex IV deficiency and impacts membrane potential driven protein transport across the inner membrane. We demonstrate that COA6 acts as a thiol-reductase to reduce disulphide bridges of critical cysteine residues in SCO1 and SCO2. Cysteines within the CX3CXNH domain of SCO2 mediate its interaction with COA6 but are dispensable for SCO2-SCO1 interaction. Our analyses define COA6 as thiol-reductase, which is essential for CuA biogenesis.

Details

show
hide
Language(s): eng - English
 Dates: 2020-02-13
 Publication Status: Published online
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1016/j.jmb.2020.01.036
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Journal of Molecular Biology
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: - Sequence Number: (in press) Start / End Page: - Identifier: -