Journal
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume 380, Issue 4, Pages 850-855Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2009.01.182
Keywords
Polyadenylation factors; mRNA processing; Protein interactions; Trypanosome diseases; Drug target
Categories
Funding
- FONCYT-PICT RE-DES [2003-00300]
- UBACyT [X-153]
- PIP-CONICET [5492]
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In trypanosomes transcription is polycistronic and individual mRNAs are generated by a trans-splicing/polyadenylation Coupled reaction. We identified a divergent trypanosome FIP1-like, a factor required for mRNA 3' end formation from yeasts to human. Here we showed that it is a nuclear protein with a speckled distribution essential for trypanosome viability. A strong interaction was found between TcFIP1-like and TcCPSF30, a component of the polyadenylation complex. We determined the specific amino acids in each protein involved in the interaction. Significant differences were found between the trypanosome interaction surface and its human counterpart. Although CPSF30/FIP1 interaction is known in other organisms, this is the first report mapping the interaction surface at the amino acid level. (C) 2009 Elsevier Inc. All rights reserved.
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