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Originally published as Genetics Published Articles Ahead of Print on October 3, 2005.
Genetics, Vol. 172, 7-15, January 2006, Copyright © 2006
doi:10.1534/genetics.105.048553
Identification and Analysis of Escherichia coli Ribonuclease E Dominant-Negative Mutants
Karoline J. Briegel, Asmaa Baker and Chaitanya Jain1
Department of Biochemistry and Molecular Biology, University of Miami Miller School of Medicine, Miami, Florida 33136
1 Corresponding author: Department of Biochemistry and Molecular Biology, University of Miami Miller School of Medicine, 1011 NW 15th St., Miami, FL 33136.
E-mail: cjain{at}med.miami.edu
The Escherichia coli (E. coli) ribonuclease E protein (RNase E) is implicated in the degradation and processing of a large fraction of RNAs in the cell. To understand RNase E function in greater detail, we developed an efficient selection method for identifying nonfunctional RNase E mutants. A subset of the mutants was found to display a dominant-negative phenotype, interfering with wild-type RNase E function. Unexpectedly, each of these mutants contained a large truncation within the carboxy terminus of RNase E. In contrast, no point mutants that conferred a dominant-negative phenotype were found. We show that a representative dominant-negative mutant can form mixed multimers with RNase E and propose a model to explain how these mutants can block wild-type RNase E function in vivo.
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