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Identification and analysis of Escherichia coli ribonuclease E dominant-negative mutants.

Authors
Type
Published Article
Journal
Genetics
0016-6731
Publisher
The Genetics Society of America
Publication Date
Volume
172
Issue
1
Pages
7–15
Identifiers
PMID: 16204212
Source
Medline

Abstract

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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