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Expression of heat shock protein 83 in Leishmania is regulated post-transcriptionally
Year:
1994
Authors :
Aly, Radi
;
.
Volume :
64
Co-Authors:
Argaman, M., Department of Membrane Research and Biophysics, The Weizmann Institute of Science, Rehovot, 76100, Israel
Aly, R., Department of Membrane Research and Biophysics, The Weizmann Institute of Science, Rehovot, 76100, Israel
Shapira, M., Department of Membrane Research and Biophysics, The Weizmann Institute of Science, Rehovot, 76100, Israel
Facilitators :
From page:
95
To page:
110
(
Total pages:
16
)
Abstract:
Mechanisms for regulation of heat shock protein (hsp) 83 expression were examined in Leishmania amazonensis. Transcripts of hsp83 accumulated upon temperature elevation; however, in contrast to non-protozoan eukaryotes (i.e. Drosophila, yeast, avian or human cells), no transcriptional activation was observed. The increase in the hsp83 mRNA level evolved from temperature induced variations in mRNA turn-over: the hsp83 transcript was rapidly degraded at normal temperatures, whereas heat shock led to its stabilization. The quick decay of the mRNA at lower temperatures was dependent on active protein synthesis. A similar pattern of regulation was observed for the transfected chloramphenicol acetyltransferase (CAT) gene, which was flanked by sequences from the hsp83 intergenic region (IR), and cloned into the pX transfection vector (pX-ICI). CAT mRNA was abundant at normal temperatures and further accumulated upon temperature elevation. The altered turn-over rates of CAT mRNA at the different temperatures were observed only in the presence of flanking hsp83 IR sequences. The increase in temperature also affected translational regulation of hsps, and synthesis of hsp83 was more efficient at 35°C than at 26°C. However, the effect on translation was transient, and the steady state level of the protein was hardly altered. © 1994.
Note:
Related Files :
Animal
Base Sequence
gene expression
Heat-Shock Proteins
Protozoan Proteins
temperature
Show More
Related Content
More details
DOI :
10.1016/0166-6851(94)90138-4
Article number:
Affiliations:
Database:
Scopus
Publication Type:
article
;
.
Language:
English
Editors' remarks:
ID:
27175
Last updated date:
02/03/2022 17:27
Creation date:
17/04/2018 00:28
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Scientific Publication
Expression of heat shock protein 83 in Leishmania is regulated post-transcriptionally
64
Argaman, M., Department of Membrane Research and Biophysics, The Weizmann Institute of Science, Rehovot, 76100, Israel
Aly, R., Department of Membrane Research and Biophysics, The Weizmann Institute of Science, Rehovot, 76100, Israel
Shapira, M., Department of Membrane Research and Biophysics, The Weizmann Institute of Science, Rehovot, 76100, Israel
Expression of heat shock protein 83 in Leishmania is regulated post-transcriptionally
Mechanisms for regulation of heat shock protein (hsp) 83 expression were examined in Leishmania amazonensis. Transcripts of hsp83 accumulated upon temperature elevation; however, in contrast to non-protozoan eukaryotes (i.e. Drosophila, yeast, avian or human cells), no transcriptional activation was observed. The increase in the hsp83 mRNA level evolved from temperature induced variations in mRNA turn-over: the hsp83 transcript was rapidly degraded at normal temperatures, whereas heat shock led to its stabilization. The quick decay of the mRNA at lower temperatures was dependent on active protein synthesis. A similar pattern of regulation was observed for the transfected chloramphenicol acetyltransferase (CAT) gene, which was flanked by sequences from the hsp83 intergenic region (IR), and cloned into the pX transfection vector (pX-ICI). CAT mRNA was abundant at normal temperatures and further accumulated upon temperature elevation. The altered turn-over rates of CAT mRNA at the different temperatures were observed only in the presence of flanking hsp83 IR sequences. The increase in temperature also affected translational regulation of hsps, and synthesis of hsp83 was more efficient at 35°C than at 26°C. However, the effect on translation was transient, and the steady state level of the protein was hardly altered. © 1994.
Scientific Publication
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