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Papers In Press, published online ahead of print October 25, 2002
J. Biol. Chem, 10.1074/jbc.M209092200
Submitted on September 5, 2002
Revised on October 22, 2002
Accepted on October 25, 2002
Instituto de Investigaciones Biotecnologicas, IIB-INTECH, San Martin, Buenos Aires 1650
Corresponding Author: cfrasch{at}iib.unsam.edu.ar
Trypanosomes, protozoan parasites causing worldwide infections in human and animals, mostly regulate protein expression through post-transcriptional mechanisms and not at the transcription initiation level. We have previously identified a Trypanosoma cruzi RNA-binding protein named TcUBP-1. This protein is involved in mRNA destabilization in vivo through binding to AU-rich elements in the 3’-untranslated region of SMUG mucin mRNAs (D’Orso, I. and Frasch A. C. (2001) J Biol Chem 276, 34801-34808). In this work we show that TcUBP-1 is part of a ~450kDa ribonucleoprotein complex with a poly(A)-binding protein and a novel 18kDa RNA-binding protein, named TcUBP-2. Recombinant TcUBP-1 and TcUBP-2 proteins recognize U-rich RNAs with similar specificity and affinity through the ~92 amino acids RNA recognition motif. TcUBPs can homo and heterodimerize in vitro through the Glycine-rich C-terminal region. This interaction was also detected in vivo by co-immunoprecipitation of the ribonucleoprotein complex and using yeast-two hybrid assay. The poly(A)-binding protein identified was shown to disrupt the formation of TcUBP-1, but not TcUBP-2, homodimers in vitro. The possible role of TcUBP-1 ligands in the pathways that govern mRNA-stability and stage-specific expression in trypanosomes is discussed.
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