NDLI: The trypanosome alternative oxidase exists as a monomer in Trypanosoma brucei mitochondria

Content Provider	Springer Nature Link
Author	Chaudhuri, Minu Ott, Robert Daniel Saha, Lipi Williams, Shuntae Hill, George C.
Copyright Year	2005
Abstract	The bloodstream forms of African trypanosomes solely depend on trypanosome alternative oxidase (TAO), for respiration. Similar to alternative oxidases (AOXs) found in plants and fungi, TAO is a membrane-bound diiron protein. Here, we investigated if TAO exists as a dimer like plant AOXs, or as a monomer like that of fungi. We have found that TAO forms a homo-dimer on a regular SDS-PAGE in the absence of any reducing agent and exists as a monomer under reducing condition. However, TAO does not form a dimer upon treatment of mitochondria with diamide. TAO was found as a higher molecular mass complex on a Blue-native gel after solubilization with digitonin. In the detergent soluble form, TAO activity was stimulated under reducing and inhibited under oxidizing condition. However, these conditions have no effect on the TAO activity in the mitochondria. Moreover, chemical cross-linking analysis revealed that TAO could not be cross-linked when present in the mitochondria. Together, it suggests that like certain other hydrophobic membrane proteins, TAO forms a dimer or oligomer when solubilized with detergents, and the TAO-dimer is SDS-resistant. However, it exists as a monomer in Trypanosoma brucei mitochondria.
Starting Page	178
Ending Page	183
Page Count	6
File Format	PDF
ISSN	09320113
Journal	Parasitology Research
Volume Number	96
Issue Number	3
e-ISSN	14321955
Language	English
Publisher	Springer-Verlag
Publisher Date	2005-04-30
Publisher Place	Berlin/Heidelberg
Access Restriction	One Nation One Subscription (ONOS)
Content Type	Text
Resource Type	Article
Subject	Infectious Diseases Veterinary Parasitology Insect Science

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