AJTMH HINARI
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Am. J. Trop. Med. Hyg., 49(5), 1993, pp. 545-551
Copyright © 1993 by The American Society of Tropical Medicine and Hygiene

This Article
Right arrow Full Text (PDF)
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 arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Lowrie, D. J.
Right arrow Articles by Ventullo, R. M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Lowrie, D. J., Jr.
Right arrow Articles by Ventullo, R. M.

The Ubiquitin-Ligase System in Trypanosoma Brucei Brucei

D. J. Lowrie, Jr., Bruce F. Giffin AND Roy M. Ventullo
Department of Biology, University of Dayton, Dayton, Ohio

The question of whether the African trypanosome Trypanosoma brucei brucei utilizes a ubiquitin-ligase system to conjugate the 8,500-dalton protein ubiquitin to other proteins has not been investigated. Using 125I-labeled ubiquitin and gel electrophoresis (sodium dodecyl sulfate and aceitc acid, urea, Triton X-100), we looked for the incorporation of label into proteins larger than ubiquitin to determine ubiquitin-ligase system activity in cytosolic and nuclear lysates of long slender, intermediate, and short stumpy bloodstream-form trypanosomes. We present data suggesting that there is cytosolic activity of a ubiquitin-ligase system in all three bloodstream forms of T. brucei brucei. There are indications that the three bloodstream forms of T. brucei brucei differ in their cytosolic ubiquitin-ligase system activity. Our assay showed no activity of this system in the nucleus of T. brucei brucei. Further studies on the ubiquitin-ligase system in T. brucei brucei may define differences between the three bloodstream forms, the parasite, and its host, leading to development of novel chemotherapeutic strategies.




This article has been cited by other articles:


Home page
 J. Biol. Chem.Home page
Z. Li, C.-B. Zou, Y. Yao, M. A. Hoyt, S. McDonough, Z. B. Mackey, P. Coffino, and C. C. Wang
An Easily Dissociated 26 S Proteasome Catalyzes an Essential Ubiquitin-mediated Protein Degradation Pathway in Trypanosoma brucei
J. Biol. Chem., May 3, 2002; 277(18): 15486 - 15498.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1993 by the American Society of Tropical Medicine and Hygiene.