This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Supplemental material
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Zíková, A.
Right arrow Articles by Stuart, K.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Zíková, A.
Right arrow Articles by Stuart, K.

 Previous Article  |  Next Article 

Eukaryotic Cell, November 2008, p. 1994-2003, Vol. 7, No. 11
1535-9778/08/$08.00+0     doi:10.1128/EC.00204-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Structural and Functional Association of Trypanosoma brucei MIX Protein with Cytochrome c Oxidase Complex {triangledown} ,{dagger}

Alena Zíková,1 Aswini K. Panigrahi,1 Alessandro D. Uboldi,2 Rachel A. Dalley,1 Emanuela Handman,2 and Kenneth Stuart1*

Seattle Biomedical Research Institute, Seattle, Washington 98109,1 Walter and Eliza Hall Institute of Medical Research, Victoria, Australia2

Received 20 June 2008/ Accepted 25 August 2008

A mitochondrial inner membrane protein, designated MIX, seems to be essential for cell viability. The deletion of both alleles was not possible, and the deletion of a single allele led to a loss of virulence and aberrant mitochondrial segregation and cell division in Leishmania major. However, the mechanism by which MIX exerts its effect has not been determined. We show here that MIX is also expressed in the mitochondrion of Trypanosoma brucei, and using RNA interference, we found that its loss leads to a phenotype that is similar to that described for Leishmania. The loss of MIX also had a major effect on cytochrome c oxidase activity, on the mitochondrial membrane potential, and on the production of mitochondrial ATP by oxidative phosphorylation. Using a tandem affinity purification tag, we found that MIX is associated with a multiprotein complex that contains subunits of the mitochondrial cytochrome c oxidase complex (respiratory complex IV), the composition of which was characterized in detail. The specific function of MIX is unknown, but it appears to be important for the function of complex IV and for mitochondrial segregation and cell division in T. brucei.

* Corresponding author. Mailing address: Seattle Biomedical Research Institute, 307 Westlake Ave. North, Suite 500, Seattle, WA 98109-5219. Phone: (206) 256-7316. Fax: (206) 256-7229. E-mail: ken.stuart{at}sbri.org

{triangledown} Published ahead of print on 5 September 2008.

{dagger} Supplemental material for this article may be found at http://ec.asm.org/.

Eukaryotic Cell, November 2008, p. 1994-2003, Vol. 7, No. 11
1535-9778/08/$08.00+0     doi:10.1128/EC.00204-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.





Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»