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Journal of Bacteriology, August 2006, p. 5831-5838, Vol. 188, No. 16
0021-9193/06/$08.00+0 doi:10.1128/JB.00630-06
Laboratory of Molecular Genetics, National Institute of Environmental Health Sciences, Research Triangle Park, North Carolina 27709,1 D. I. Ivanovsky Institute of Virology, Russian Academy of Medical Science, Moscow 123098, Russia2
Received 3 May 2006/ Accepted 31 May 2006
The Hot (homolog of theta) protein of bacteriophage P1 can substitute for the Escherichia coli DNA polymerase III
subunit, as evidenced by its stabilizing effect on certain dnaQ mutants that carry an unstable polymerase III
proofreading subunit (antimutator effect). Here, we show that Hot can also cause an increase in the mutability of various E. coli strains (mutator effect). The hot mutator effect differs from the one caused by the lack of
. Experiments using chimeric
/Hot proteins containing various domains of Hot and
along with a series of point mutants show that both N- and C-terminal parts of each protein are important for stabilizing the
subunit. In contrast, the N-terminal part of Hot appears uniquely responsible for its mutator activity.
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