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J. Biol. Chem., Vol. 278, Issue 18, 15771-15777, May 2, 2003
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From the Department of Biology, Technion-Israel Institute of
Technology, Haifa 32000, Israel
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.
RNA Polyadenylation and Degradation in Cyanobacteria Are Similar
to the Chloroplast but Different from Escherichia
coli*
*
This work was supported by grants from the Israel Science
Foundation and the Israel-USA Binational Agriculture Research and Development Foundation.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed. Tel.: 972-4-8293171;
Fax: 972-4-8295587; E-mail: gadis@tx.technion.ac.il.
Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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