Nucleic Acids Research, 2001, Vol. 29, No. 9 1864-1871
© 2001 Oxford University Press
Cleavage of poly(A) tails on the 3'-end of RNA by ribonuclease E of Escherichia coli
Astbury Centre for Structural Molecular Biology, Faculty of Biological Sciences, University of Leeds, Leeds LS2 9JT, UK and 1Institute of Microbiology and Genetics, Vienna Biocenter, A-1030 Vienna, Austria
RNase E initiates the decay of Escherichia coli RNAs by cutting them internally near their 5'-end and is a component of the RNA degradosome complex, which also contains the 3'-exonuclease PNPase. Recently, RNase E has been shown to be able to remove poly(A) tails by what has been described as an exonucleolytic process that can be blocked by the presence of a phosphate group on the 3'-end of the RNA. We show here, however, that poly(A) tail removal by RNase E is in fact an endonucleolytic process that is regulated by the phosphorylation status at the 5'- but not the 3'-end of RNA. The rate of poly(A) tail removal by RNase E was found to be 30-fold greater when the 5'-terminus of RNA substrates was converted from a triphosphate to monophosphate group. This finding prompted us to re-analyse the contributions of the ribonucleolytic activities within the degradosome to 3' attack since previous studies had only used substrates that had a triphosphate group on their 5'-end. Our results indicate that RNase E associated with the degradosome may contribute to the removal of poly(A) tails from 5'-monophosphorylated RNAs, but this is only likely to be significant should their attack by PNPase be blocked.
* To whom correspondence should be addressed. Tel: +44 113 233 3109; Fax: +44 113 233 1407; Email: k.j.mcdowall{at}leeds.ac.uk Present addresses: A. P. Walsh, MRC Laboratory of Molecular Biology, Cambridge CB2 2QH, UKM. R. Tock, Department of Chemistry, University of Sheffield, Sheffield S3 7HF, UK The authors wish it to be known that, in their opinion, the first two authors should be regarded as joint First Authors
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