PMID:11328869
| Citation |
Walsh, AP, Tock, MR, Mallen, MH, Kaberdin, VR, von Gabain, A and McDowall, KJ (2001) Cleavage of poly(A) tails on the 3'-end of RNA by ribonuclease E of Escherichia coli. Nucleic Acids Res. 29:1864-71 |
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| Abstract |
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. |
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| Keywords |
3' Untranslated Regions; Base Sequence; Endoribonucleases/metabolism; Escherichia coli/enzymology; Kinetics; Molecular Sequence Data; Nucleic Acid Conformation; Oligonucleotides/chemistry; Oligonucleotides/metabolism; Phosphorylation; Poly A/metabolism; RNA, Messenger/chemistry; RNA, Messenger/metabolism |
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