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פותח על ידי קלירמאש פתרונות בע"מ -
A regulatory role for the 5′ and 3′ untranslated regions in differential expression of hsp83 in Leishmania
Year:
1994
Source of publication :
Nucleic Acids Research
Authors :
עלי, ראדי
;
.
Volume :
22
Co-Authors:
Aly, R., Department of Membrane Research and Biophysics, Weizmann Institute of Science, Rehovot 76100, Israel
Argaman, M., Department of Membrane Research and Biophysics, Weizmann Institute of Science, Rehovot 76100, Israel
Halman, S., Department of Membrane Research and Biophysics, Weizmann Institute of Science, Rehovot 76100, Israel
Shapira, M., Department of Membrane Research and Biophysics, Weizmann Institute of Science, Rehovot 76100, Israel
Facilitators :
From page:
2922
To page:
2929
(
Total pages:
8
)
Abstract:
Exposure of Leishmania promastigotes to temperatures typical of mammals results in a stress response, which is accompanied by an increase in the steady state level of heat shock transcripts and their translation. Accumulation of the heat shock protein (hsp83) mRNA occurs due to differential decay rates at the altered temperatures, while transcription is unaffected. A similar pattern of post-transcriptional regulation was observed for a transfected chloramphenicol acetyltransferase (CAT) gene, which was flanked at both ends by intergenic regions (IR) of hsp83. Shortening the 5′ untranslated region (UTR) by 100 nts produced an active CAT enzyme, but abolished the temperature-dependent regulation of the CAT - hsp83 mRNA turn-over. The 3′ UTR is also involved in the temperature-dependent degradation of hsp83 mRNA, since exchange of the hsp83 3′ UTR with a parallel fragment from a non-heat shock gene abolished the differential turn-over of CAT mRNA. Thus, the regulated decay of hsp83 mRNA is controlled by sequence or conformational elements present in both upstream and downstream UTRs. Like the endogenous hsp83, translation of CAT mRNA which contained hsp83 UTRs was higher at 35°C. This was observed only with transcripts in which stability increased at elevated temperatures. Modifications which abolished the temperature dependence of CAT mRNA decay, eliminated its elevated translation at the higher temperatures. The correlation suggests a mechanistic link between the translational machinery and mRNA stability. © 1994 Oxford University Press.
Note:
Related Files :
Animal
chromosome mapping
Drug Stability
Mammalia
temperature
עוד תגיות
תוכן קשור
More details
DOI :
10.1093/nar/22.15.2922
Article number:
Affiliations:
Database:
סקופוס
Publication Type:
מאמר
;
.
Language:
אנגלית
Editors' remarks:
ID:
25278
Last updated date:
02/03/2022 17:27
Creation date:
17/04/2018 00:13
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Scientific Publication
A regulatory role for the 5′ and 3′ untranslated regions in differential expression of hsp83 in Leishmania
22
Aly, R., Department of Membrane Research and Biophysics, Weizmann Institute of Science, Rehovot 76100, Israel
Argaman, M., Department of Membrane Research and Biophysics, Weizmann Institute of Science, Rehovot 76100, Israel
Halman, S., Department of Membrane Research and Biophysics, Weizmann Institute of Science, Rehovot 76100, Israel
Shapira, M., Department of Membrane Research and Biophysics, Weizmann Institute of Science, Rehovot 76100, Israel
A regulatory role for the 5′ and 3′ untranslated regions in differential expression of hsp83 in Leishmania
Exposure of Leishmania promastigotes to temperatures typical of mammals results in a stress response, which is accompanied by an increase in the steady state level of heat shock transcripts and their translation. Accumulation of the heat shock protein (hsp83) mRNA occurs due to differential decay rates at the altered temperatures, while transcription is unaffected. A similar pattern of post-transcriptional regulation was observed for a transfected chloramphenicol acetyltransferase (CAT) gene, which was flanked at both ends by intergenic regions (IR) of hsp83. Shortening the 5′ untranslated region (UTR) by 100 nts produced an active CAT enzyme, but abolished the temperature-dependent regulation of the CAT - hsp83 mRNA turn-over. The 3′ UTR is also involved in the temperature-dependent degradation of hsp83 mRNA, since exchange of the hsp83 3′ UTR with a parallel fragment from a non-heat shock gene abolished the differential turn-over of CAT mRNA. Thus, the regulated decay of hsp83 mRNA is controlled by sequence or conformational elements present in both upstream and downstream UTRs. Like the endogenous hsp83, translation of CAT mRNA which contained hsp83 UTRs was higher at 35°C. This was observed only with transcripts in which stability increased at elevated temperatures. Modifications which abolished the temperature dependence of CAT mRNA decay, eliminated its elevated translation at the higher temperatures. The correlation suggests a mechanistic link between the translational machinery and mRNA stability. © 1994 Oxford University Press.
Scientific Publication
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