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Originally published In Press as doi:10.1074/jbc.M200174200 on February 20, 2002
J. Biol. Chem., Vol. 277, Issue 19, 16489-16497, May 10, 2002
Comparison of the Post-transcriptional Regulation of the
mRNAs for the Surface Proteins PSA (GP46) and MSP (GP63) of
Leishmania chagasi*
Karen S.
Myung §,
Jeffrey K.
Beetham ¶,
Mary E.
Wilson§ ** , and
John E.
Donelson §§§
From the Departments of Biochemistry,
Microbiology, and ** Internal Medicine and the
§ Medical Scientist Training Program, University of Iowa and
the  Veterans Affairs Medical Center,
Iowa City, Iowa 52242
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 kilobases were cloned immediately downstream
of a -galactosidase reporter gene in a plasmid, 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 the regulation of mRNAs encoding the dipeptide
(EP) and pentapeptide (GPEET) repeat proteins in Trypanosoma
brucei that involves interactions between positive and negative
regulatory elements in the 3'-UTR.
*
This work was supported in part by National Institutes of
Health Grants AI32135 and AI43050 and a Veterans Affairs Merit Review grant.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.
¶
Present address: Dept. of Veterinary Pathology, Iowa State
University, Ames, IA 50011.
§§
To whom correspondence should be addressed. Tel.: 319-335-7934;
Fax: 319-353-4204; E-mail: john-donelson@uiowa.edu.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.

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