Ribonuclease E is a 5′-end-dependent endonuclease

George A. Mackie ()
Additional contact information
George A. Mackie: University of British Columbia

Nature, 1998, vol. 395, issue 6703, 720-724

Abstract: Abstract The selective degradation of messenger RNAs enables cells to regulate the levels of particular mRNAs in response to changes in the environment. Ribonuclease (RNase) E (ref. 1), a single-strand-specific endonuclease2,3,4 that is found in a multi-enzyme complex known as the ‘degradosome’5,6,7, initiates the degradation of many mRNAs in Escherichia coli3,8,9. Its relative lack of sequence specificity and the presence of many potential cleavage sites in mRNA substrates2,3 cannot explain why mRNA decay frequently proceeds in a net 5′-to-3′ direction9,10,11. I have prepared covalently closed circular derivatives of natural substrates, the rpsT mRNA encoding ribosomal protein S20 (ref. 2) and the 9S precursor to 5S ribosomal RNA1,12, and find that these derivatives are considerably more resistant to cleavage in vitro by RNase E than are linear molecules. Moreover, antisense oligo-deoxynucleotides complementary to the 5′ end of linear substrates significantly reduce the latter's susceptibility to attack by RNase E. Finally, natural substrates with terminal 5′-triphosphate groups are poorly cleaved by RNase E in vitro, whereas 5′ monophosphorylated substrates are strongly preferred (compare with ref. 13). These results show that RNase E has inherent vectorial properties, with its activity depending on the 5′ end of its substrates; this can account for the direction of mRNA decay in E. coli, the phenomenon of ‘all or none’ mRNA decay, and the stabilization provided by 5′ stem–loop structures14,15,16,17.

Date: 1998
References: Add references at CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/27246 Abstract (text/html)
Access to the full text of the articles in this series is restricted.

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:395:y:1998:i:6703:d:10.1038_27246

Ordering information: This journal article can be ordered from
https://www.nature.com/

DOI: 10.1038/27246

Access Statistics for this article

Nature is currently edited by Magdalena Skipper

More articles in Nature from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().