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Papers In Press, published online ahead of print February 20, 2002
Department of Biochemistry, University of Iowa, Iowa City, Iowa 52242
Corresponding Author: john-donelson{at}uiowa.edu
MSP (GP63) and PSA (GP46) are abundant 63- and 46-kDa glycolipid-anchored proteins on the surface of the promastigote form of most Leishmania species. MSP is a zinc metalloprotease that confers resistance to host complement-mediated lysis. PSA contains internal repeats of 24 amino acids and its function is unknown. The steady state levels of mRNAs for both glycoproteins are regulated post-transcriptionally, resulting in about a 30-fold increase as Leishmania chagasi promastigotes grow in vitro from logarithmic phase to stationary phase. Previous studies showed the 3' untranslated regions (3' UTRs) of these mRNAs are essential for this post-transcriptional regulation. These two 3' UTRs of 1.0 and 1.3 kb were cloned in a plasmid immediately downstream of a
J. Biol. Chem, 10.1074/jbc.M200174200
Submitted on January 8, 2002
Revised on February 1, 2002
Accepted on February 20, 2002
Comparison of the post-transcriptional regulation of the mRNAs for the surface proteins PSA (GP46) and MSP (GP63) of Leishmania chagasi
-galactosidase reporter gene and segments were systematically deleted to examine which portions of the 3' UTRs contribute to the post-transcriptional regulation. The 92-nucleotide segment of greatest similarity between the two 3' UTRs was deleted without loss of regulation, but the segments flanking this similarity region have positive regulatory elements essential for the regulation. We propose that similar, but non-identical, molecular mechanisms regulate the parallel expression of these two L. chagasi mRNAs despite their lack of sequence identity. These post-transcriptional mechanisms resemble the mechanism recently suggested for EP/GPEET mRNA regulation in Trypanosoma brucei that involves interactions between positive and negative regulatory elements in the 3' UTR.
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