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פותח על ידי קלירמאש פתרונות בע"מ -
RNA polyadenylation and degradation in cyanobacteria are similar to the chloroplast but different from Escherichia coli
Year:
2003
Source of publication :
Journal of Biological Chemistry
Authors :
ציפור, גדי
;
.
Volume :
278
Co-Authors:
Rott, R., Department of Biology, Technion-Israel Inst. of Technology, Haifa 32000, Israel
Zipor, G., Department of Biology, Technion-Israel Inst. of Technology, Haifa 32000, Israel
Portnoy, V., Department of Biology, Technion-Israel Inst. of Technology, Haifa 32000, Israel
Liveanu, V., Department of Biology, Technion-Israel Inst. of Technology, Haifa 32000, Israel
Schuster, G., Department of Biology, Technion-Israel Inst. of Technology, Haifa 32000, Israel
Facilitators :
From page:
15771
To page:
15777
(
Total pages:
7
)
Abstract:
The mechanism of RNA degradation in Escherichia coli involves endonucleolytic cleavage, polyadenylation of the cleavage product by poly(A) polymerase, and exonucleolytic degradation by the exoribonucleases, polynucleotide phosphorylase (PNPase) and RNase II. The poly(A) tails are homogenous, containing only adenosines in most of the growth conditions. In the chloroplast, however, the same enzyme, PNPase, polyadenylates and degrades the RNA molecule; there is no equivalent for the E. coli poly(A) polymerase enzyme. Because cyanobacteria is a prokaryote believed to be related to the evolutionary ancestor of the chloroplast, we asked whether the molecular mechanism of RNA polyadenylation in the Synechocystis PCC6803 cyanobacteria is similar to that in E. coli or the chloroplast. We found that RNA polyadenylation in Synechocystis is similar to that in the chloroplast but different from E. coli. No poly(A) polymerase enzyme exists, and polyadenylation is performed by PNPase, resulting in heterogeneous poly(A)-rich tails. These heterogeneous tails were found in the amino acid coding region, the 5′ and 3′ untranslated regions of mRNAs, as well as in rRNA and the single intron located at the tRNAfmet. Furthermore, unlike E. coli, the inactivation of PNPase or RNase II genes caused lethality. Together, our results show that the RNA polyadenylation and degradation mechanisms in cyanobacteria and chloroplast are very similar to each other but different from E. coli.
Note:
Related Files :
bacteria
Biochemistry
chlorophyll
enzymes
Genetics
molecular genetics
RNA
עוד תגיות
תוכן קשור
More details
DOI :
10.1074/jbc.M211571200
Article number:
Affiliations:
Database:
סקופוס
Publication Type:
מאמר
;
.
Language:
אנגלית
Editors' remarks:
ID:
20036
Last updated date:
02/03/2022 17:27
Creation date:
16/04/2018 23:33
Scientific Publication
RNA polyadenylation and degradation in cyanobacteria are similar to the chloroplast but different from Escherichia coli
278
Rott, R., Department of Biology, Technion-Israel Inst. of Technology, Haifa 32000, Israel
Zipor, G., Department of Biology, Technion-Israel Inst. of Technology, Haifa 32000, Israel
Portnoy, V., Department of Biology, Technion-Israel Inst. of Technology, Haifa 32000, Israel
Liveanu, V., Department of Biology, Technion-Israel Inst. of Technology, Haifa 32000, Israel
Schuster, G., Department of Biology, Technion-Israel Inst. of Technology, Haifa 32000, Israel
RNA polyadenylation and degradation in cyanobacteria are similar to the chloroplast but different from Escherichia coli
The mechanism of RNA degradation in Escherichia coli involves endonucleolytic cleavage, polyadenylation of the cleavage product by poly(A) polymerase, and exonucleolytic degradation by the exoribonucleases, polynucleotide phosphorylase (PNPase) and RNase II. The poly(A) tails are homogenous, containing only adenosines in most of the growth conditions. In the chloroplast, however, the same enzyme, PNPase, polyadenylates and degrades the RNA molecule; there is no equivalent for the E. coli poly(A) polymerase enzyme. Because cyanobacteria is a prokaryote believed to be related to the evolutionary ancestor of the chloroplast, we asked whether the molecular mechanism of RNA polyadenylation in the Synechocystis PCC6803 cyanobacteria is similar to that in E. coli or the chloroplast. We found that RNA polyadenylation in Synechocystis is similar to that in the chloroplast but different from E. coli. No poly(A) polymerase enzyme exists, and polyadenylation is performed by PNPase, resulting in heterogeneous poly(A)-rich tails. These heterogeneous tails were found in the amino acid coding region, the 5′ and 3′ untranslated regions of mRNAs, as well as in rRNA and the single intron located at the tRNAfmet. Furthermore, unlike E. coli, the inactivation of PNPase or RNase II genes caused lethality. Together, our results show that the RNA polyadenylation and degradation mechanisms in cyanobacteria and chloroplast are very similar to each other but different from E. coli.
Scientific Publication
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