Some trypanosomatid parasites cause lethal human diseases and therefore are intensely investigated. Curiously, these unicellular eukaryotes transcribe their genes polycistronically like prokaryotes and use a mechanism called spliced leader trans splicing to generate individual mRNA molecules.
While this essential process is carried out by the intron-removing spliceosome, it is likely that it also requires dedicated factors. However, trypanosomatid spliceosomes have not been well characterized, mainly because the protein sequences of these organisms are extraordinarily divergent and typically cannot be identified by similarity. To circumvent this problem, Arthur Gu¨ nzl of the University of Connecticut Health Center, Farmington, et al. epitope-tagged a known splicing factor in Trypanosoma brucei and used the tag to tandem affinity purify the trypanosome splicing machinery from cell-free extracts. "Employing mass spectrometry, we identified a total of 47 proteins which included nearly all known spliceosomal proteins of the parasite but also several proteins which appear to be novel, parasitespecific factors. The focus is now on these latter proteins because they may have a trans splicingspecific function and, since SL trans splicing does not occur in humans, they are potential [and urgently needed] drug targets."
(D. L. Ambrósio, J. H. Lee, A. K. Panigrahi, T. N. Nguyen, R. M. B. Cicarelli, and A. Günzl. 2009. Spliceosomal proteomics in Trypanosoma brucei reveal new RNA splicing factors. Eukaryot. Cell 8:990-1000.) |
Journal Highlights 
Facebook
del.icio.us
Digg
Furl 
Yahoo!My Web
StumbleUpon
Google
Technorati 
reddit
Twitter
