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Virulence in bacteriophage Mu: a case of trans‐dominant proteolysis by the Escherichia coli Clp serine protease.
Author(s) -
Geuskens V.,
MhammediAlaoui A.,
Desmet L.,
Toussaint A.
Publication year - 1992
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1992.tb05619.x
Subject(s) - transposition (logic) , biology , escherichia coli , virulence , serine protease , transposable element , genetics , microbiology and biotechnology , gene , protease , philosophy , genome , biochemistry , linguistics , enzyme
The importance of proteases in gene regulation is well documented in both prokaryotic and eukaryotic systems. Here we describe the first example of genetic regulation controlled by the Escherichia coli Clp ATP‐dependent serine protease. Virulent mutants of bacteriophage Mu, which carry a particular mutation in their repressor gene (vir mutation), successfully infect Mu lysogens and induce the resident Mu prophage. We show that the mutated repressors have an abnormally short half‐life due to an increased susceptibility to Clp‐dependent degradation. This susceptibility is communicated to the wild type repressor present in the same cell, which provides the Muvir phages with their trans‐dominant phenotype. To our knowledge this is the first case where the instability of a mutant protein is shown to trigger the degradation of its wild type parent.