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J. Biol. Chem., Vol. 277, Issue 52, 50520-50528, December 27, 2002
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From the Instituto de Investigaciones
Biotecnológicas-Instituto Tecnológico de Chascomús,
CONICET-UNSAM, 1650 San Martín, Provincia de Buenos Aires,
Argentina
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, 34801-34809). In this work
we show that TcUBP-1 is part of an ~450-kDa ribonucleoprotein complex
with a poly(A)-binding protein and a novel 18-kDa 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 acid 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.
The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EBI Data Bank with accession number(s) AF497746.
TcUBP-1, an mRNA Destabilizing Factor from Trypanosomes,
Homodimerizes and Interacts with Novel AU-rich Element- and
Poly(A)-binding Proteins Forming a Ribonucleoprotein Complex*
and
*
This work was supported in part by grants from the World
Bank/UNDP/WHO Special Program for Research and Training in Tropical Diseases (Tropical Disease Research) and by the Agencia Nacional de Promoción Científica y Tecnológica (Argentina).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Supported in part by an International Research Scholars Grant from
the Howard Hughes Medical Institute and a fellowship from the John
Simon Guggenheim Memorial Foundation. Researcher from the National
Research Council (CONICET), Argentina.
§
Research fellow from the National Research Council (CONICET),
Argentina. To whom correspondence should be addressed: IIB-UNSAM, INTI,
Av. Gral. Paz s/n, Edificio 24, Casilla de Correo 30, 1650 San
Martín, Provincia de Buenos Aires, Argentina. Tel.:
54-11-4580-7255; Fax: 54-11-4752-9639; E-mail:
cfrasch@iib.unsam.edu.ar.
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