Expression of trans-sialidase and 85-kDa glycoprotein genes in Trypanosoma cruzi is differentially regulated at the post-transcriptional level by labile protein factors

被引:47
作者
Abuin, G
Freitas, LHG
Colli, W
Alves, MJM
Schenkman, S
机构
[1] Univ Fed Sao Paulo, Escola Paulista Med, Dept Microbiol Immunol & Parasitol, BR-04023062 Sao Paulo, Brazil
[2] Univ Sao Paulo, Inst Quim, Dept Bioquim, BR-05599970 Sao Paulo, Brazil
关键词
D O I
10.1074/jbc.274.19.13041
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
To adapt to different environments, Trypanosoma cruzi, the protozoan parasite that causes Chagas' disease, expresses a different set of proteins during development, To bean 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.
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页码:13041 / 13047
页数:7
相关论文
共 62 条
[1]   A SURFACE-ANTIGEN OF TRYPANOSOMA-CRUZI INVOLVED IN CELL INVASION (TC-85) IS HETEROGENEOUS IN EXPRESSION AND MOLECULAR CONSTITUTION [J].
ABUIN, G ;
COLLI, W ;
DESOUZA, W ;
ALVES, MJM .
MOLECULAR AND BIOCHEMICAL PARASITOLOGY, 1989, 35 (03) :229-238
[2]  
ALVES MJM, 1986, MOL BIOCHEM PARASIT, V21, P75, DOI 10.1016/0166-6851(86)90081-2
[3]   TRYPANOSOMA-RANGELI - SEQUENCE-ANALYSIS OF BETA-TUBULIN GENE SUGGESTS CLOSER RELATIONSHIP TO TRYPANOSOMA-BRUCEI THAN TO TRYPANOSOMA-CRUZI [J].
AMORIM, MI ;
MOMEN, H ;
TRAUBCSEKO, YM .
ACTA TROPICA, 1993, 53 (02) :99-105
[4]  
ATWATER JA, 1990, ANNU REV GENET, V24, P519
[5]   CELL SUBSTRATE ADHESION DURING TRYPANOSOMA-CRUZI DIFFERENTIATION [J].
BONALDO, MC ;
SOUTOPADRON, T ;
DESOUZA, W ;
GOLDENBERG, S .
JOURNAL OF CELL BIOLOGY, 1988, 106 (04) :1349-1358
[6]   TRYPANOSOMA-CRUZI ATTACHMENT TO LYMPHOCYTE MUSCARINIC CHOLINERGIC AND BETA-ADRENERGIC RECEPTORS MODULATES INTRACELLULAR SIGNAL TRANSDUCTION [J].
BORDA, ES ;
STERINBORDA, LJ ;
PASCUAL, JO ;
GORELIK, G ;
FELIX, JC ;
VONKREUTER, BF ;
SANTOSBUCH, CA .
MOLECULAR AND BIOCHEMICAL PARASITOLOGY, 1991, 47 (01) :91-100
[7]   THE INTERACTION OF A TRYPANOSOMA-CRUZI SURFACE PROTEIN WITH VERO CELLS AND ITS RELATIONSHIP WITH PARASITE ADHESION [J].
BOSCHETTI, MA ;
PIRAS, MM ;
HENRIQUEZ, D ;
PIRAS, R .
MOLECULAR AND BIOCHEMICAL PARASITOLOGY, 1987, 24 (02) :175-184
[8]  
CamargO E. P., 1964, Revista do Instituto de Medicina Tropical de Sao Paulo, V6, P93
[9]  
CHOMCZYNSKI P, 1987, ANAL BIOCHEM, V162, P156, DOI 10.1016/0003-2697(87)90021-2
[10]   TRYPANOSOMA-CRUZI TRANS-SIALIDASE - ENHANCEMENT OF VIRULENCE IN A MURINE MODEL OF CHAGAS-DISEASE [J].
CHUENKOVA, M ;
PEREIRA, MEA .
JOURNAL OF EXPERIMENTAL MEDICINE, 1995, 181 (05) :1693-1703