MCP Danish Cancer Society
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
 QUICK SEARCH:   [advanced]


     


A more recent version of this article appeared on March 1, 2008.
This Article
Right arrow Full Text (PDF)
Right arrow Supplemental Data
Right arrow All Versions of this Article:
M700430-MCP200v1
7/3/534    most recent
Right arrow Submit a response
Right arrow Alert me when this article is cited
Right arrow Alert me when eLetters are posted
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
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 arrow Glossary
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Panigrahi, A. K.
Right arrow Articles by Stuart, K. D.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Panigrahi, A. K.
Right arrow Articles by Stuart, K. D.
Social Bookmarking
 Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Submitted on September 11, 2007
Revised on December 4, 2007
Accepted on December 11, 2007

Mitochondrial complexes in trypanosoma brucei: a novel complex and a unique oxidoreductase complex

Aswini K. Panigrahi, Alena Zíková, Rachel A. Dalley, Nathalie Acestor, Yuko Ogata, Atashi Anupama, Peter J. Myler, and Kenneth D. Stuart

Seattle Biomedical Research Institute, Seattle, WA 98109

Corresponding Author: ken.stuart{at}sbri.org

African trypanosomes, early diverged eukaryotes and the agents of sleeping sickness, have several basic cellular processes that are remarkably divergent from those in their mammalian hosts. They have large mitochondria and switch between oxidative phosphorylation and glycolysis as the major pathways for energy generation during their life cycle. We report here the identification and characterization of several multi-protein mitochondrial complexes from procyclic form Trypanosoma brucei. These were identified and purified using a panel of monoclonal antibodies that were generated against a sub-mitochondrial protein fraction and using TAP-tag affinity chromatography, and localized within the cells by immunofluorescence. Protein composition analyses by mass spectrometry revealed substantial divergence of oxidoreductase complex from other organisms, and identified a novel complex that may have function associated with nucleic acids. The relationship to divergent physiological processes in these pathogens is discussed.


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
J. Biol. Chem.Home page
J. C. Fisk, M. L. Ammerman, V. Presnyak, and L. K. Read
TbRGG2, an Essential RNA Editing Accessory Factor in Two Trypanosoma brucei Life Cycle Stages
J. Biol. Chem., August 22, 2008; 283(34): 23016 - 23025.
[Abstract] [Full Text] [PDF]


Home page
Mol. Cell. ProteomicsHome page
A. Zikova, A. K. Panigrahi, R. A. Dalley, N. Acestor, A. Anupama, Y. Ogata, P. J. Myler, and K. Stuart
Trypanosoma brucei Mitochondrial Ribosomes: Affinity Purification and Component Identification by Mass Spectrometry
Mol. Cell. Proteomics, July 1, 2008; 7(7): 1286 - 1296.
[Abstract] [Full Text] [PDF]


Home page
RNAHome page
H. Hashimi, A. Zikova, A. K. Panigrahi, K. D. Stuart, and J. Lukes
TbRGG1, an essential protein involved in kinetoplastid RNA metabolism that is associated with a novel multiprotein complex
RNA, May 1, 2008; 14(5): 970 - 980.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
 All ASBMB Journals   Journal of Biological Chemistry 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2007 by the American Society for Biochemistry and Molecular Biology.