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J Biol Chem, Vol. 274, Issue 19, 13041-13047, May 7, 1999
From the To adapt to different environments,
Trypanosoma cruzi, the protozoan parasite that causes
Chagas' disease, expresses a different set of proteins during
development. To begin to understand the mechanism that controls this
differential gene expression, we have analyzed the levels of
amastin and trans-sialidase mRNAs and the
mRNAs encoding members of the 85-kDa glycoprotein gene family,
which are differentially expressed in the T. cruzi stages found in the mammalian host. Amastin mRNA is expressed
predominantly in intracellular and proliferative amastigotes.
trans-Sialidase mRNAs are found mostly in forms
undergoing transformation from amastigotes to trypomastigotes inside
infected cells, whereas mRNAs encoding the 85-kDa glycoproteins
appear only in the infective trypomastigotes released from the cells.
The genes coding for these mRNA species are constitutively
transcribed in all stages of T. cruzi cells, suggesting
that expression is controlled post-transcriptionally during
differentiation. Inhibition of transcription by actinomycin D revealed
that each mRNA species has a relatively long half-life in stages
where it accumulates. In the case of the trans-sialidase and 85-kDa glycoprotein genes, mRNA accumulation was induced by treatment with the protein synthesis inhibitor cycloheximide at the
stages that preceded the normal accumulation. Therefore, mRNA stabilization may account for mRNA accumulation. mRNA
degradation could be promoted by proteins with high turnover, or
stabilization could be promoted by forming a complex with the
translational machinery at defined times in development. Identification
of the factors that induce mRNA degradation or stabilization is
essential to the understanding of control of gene expression in these organisms.
Expression of trans-Sialidase and 85-kDa Glycoprotein
Genes in Trypanosoma cruzi Is Differentially Regulated at
the Post-transcriptional Level by Labile Protein Factors
,,
Departamento de Microbiologia, Imunologia e
Parasitologia, Escola Paulista de Medicina, Universidade Federal de
São Paulo, R. Botucatu 862 8o A, 04023-062 São
Paulo, São Paulo, Brasil and the ¶ Departamento de
Bioquímica, Instituto de Química, Universidade de
São Paulo, 05599-970 São Paulo, Brasil
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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