Escherichia coli endoribonuclease RNase E: autoregulation of expression and site-specific cleavage of mRNA
Article first published online: 27 OCT 2006
Volume 9, Issue 3, pages 557–568, August 1993
How to Cite
Mudd, E. A. and Higgins, C. F. (1993), Escherichia coli endoribonuclease RNase E: autoregulation of expression and site-specific cleavage of mRNA. Molecular Microbiology, 9: 557–568. doi: 10.1111/j.1365-2958.1993.tb01716.x
- Issue published online: 27 OCT 2006
- Article first published online: 27 OCT 2006
- Received 11 March, 1993; revised and accepted 4 May, 1993.
Mutations in the Escherichia coli rne (ams) gene have a general effect on the rate of mRNA decay in vivo. Using antibodies we have shown that the product of the rne gene is a polypeptide of relative mobility 180kDa. However, proteolytic fragments as small as 70kDa, which can arise during purification, also exhibit RNase E activity, in vitro studies demonstrate that the rne gene product, RNase E, is an endoribonuclease that cleaves mRNA at specific sites. RNase E cleaves rne mRNA and autoregulates the expression of the rne gene. In addition we demonstrate RNase E-dependent endonucleolytic cleavage of ompA mRNA, at a site known to be rate-determining for degradation and reported to be cieaved by RNase K. Our data are consistent with RNase K being a proteolytic fragment of RNase E.