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Eukaryotic Cell, July 2009, p. 921, Vol. 8, No. 7
1535-9778/09/$08.00+0     doi:10.1128/EC.00158-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

SPOTLIGHT

Article of Significant Interest Selected from This Issue by the Editors

Newly Identified, Spliceosomal Proteins To Be Studied in Trypanosomes

Trypanosomatid parasites process all nuclear pre-mRNA by spliced leader trans splicing, which is an essential step in mRNA maturation and expression. In addition, trypanosomatids are capable of intron removal by conventional cis splicing. Despite the relevance of RNA splicing to the parasites, their spliceosomal protein machinery is not well characterized. This is surprising because studies with Trypanosoma brucei have shown that the building blocks of the spliceosome, the small nuclear ribonucleoprotein particles (snRNPs), deviate substantially from their human counterparts. Ambrósio et al. (p. 990-1000) tagged the canonical core snRNP protein SmD1 in T. brucei and used tandem affinity purification and mass spectrometry to isolate and identify copurified proteins. They present a set of 47 proteins, containing nearly all the snRNP proteins that have been characterized or putatively annotated in the T. brucei genome thus far, several newly identified orthologues of known splicing factors, an apparently novel and essential U5-specific snRNP protein, as well as a subset of proteins which, by primary structure analysis, appear to be parasite-specific factors.

Eukaryotic Cell, July 2009, p. 921, Vol. 8, No. 7
1535-9778/09/$08.00+0     doi:10.1128/EC.00158-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.




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