The FIP-1 like polyadenylation factor in trypanosomes and the structural basis for its interaction with CPSF30

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...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 2009-03, Vol.380 (4), p.850-855
Main Authors: Bercovich, Natalia, Levin, Mariano J., Vazquez, Martin P.
Format: Article
Language:English
Subjects:
60 APPLIED LIFE SCIENCES
Amino Acid Sequence
AMINO ACIDS
Animals
Cleavage And Polyadenylation Specificity Factor - chemistry
Cleavage And Polyadenylation Specificity Factor - genetics
Cleavage And Polyadenylation Specificity Factor - metabolism
Drug target
Molecular Sequence Data
mRNA Cleavage and Polyadenylation Factors - chemistry
mRNA Cleavage and Polyadenylation Factors - genetics
mRNA Cleavage and Polyadenylation Factors - metabolism
mRNA processing
Polyadenylation
Polyadenylation factors
POLYMERASE CHAIN REACTION
Protein interactions
PROTEINS
SPECIFICITY
SPLICING
STRONG INTERACTIONS
SURFACES
TRANSCRIPTION
Trypanosoma
Trypanosoma brucei brucei - metabolism
Trypanosoma brucei brucei - physiology
Trypanosoma cruzi - metabolism
Trypanosoma cruzi - physiology
Trypanosome diseases
TRYPANOSOMES
Two-Hybrid System Techniques
YEASTS
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Summary: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.
ISSN:0006-291X
1090-2104
DOI:10.1016/j.bbrc.2009.01.182