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Escherichia coli endoribonuclease RNase E: autoregulation of expression and site‐specific cleavage of mRNA
Author(s) -
Mudd Elisabeth A.,
Higgins Christopher F.
Publication year - 1993
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.1993.tb01716.x
Subject(s) - endoribonuclease , biology , rnase p , escherichia coli , ribonuclease iii , messenger rna , cleavage (geology) , microbiology and biotechnology , genetics , rna , gene , rna interference , paleontology , fracture (geology)
Summary 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.