Escherichia coli integration host factor stabilizes bacteriophage Mu repressor interactions with operator DNA in vitro.
Using gel retardation and DNase I protection techniques, we have demonstrated that the Escherichia coli integration host factor (IHF) stabilizes the interaction between Mu repressor and its cognate operator-binding sites in vitro. These results are discussed in terms of a model in which IHF may commit the phage to the lytic or lysogenic pathway depending on the occupancy of the operator sites by the repressor.
Alazard
R
R
Centre de Recherches en Biochimie et Génétique Cellulaires, Toulouse, France.
Bétermier
M
M
Chandler
M
M
D001426:Bacterial Proteins / Q000378:metabolism*; D010583:Bacteriophage mu / Q000378:metabolism*; D001483:Base Sequence; D004279:DNA, Viral / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000378:metabolism*; D003850:Deoxyribonuclease I; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli; D034982:Integration Host Factors; D008969:Molecular Sequence Data; D009875:Operator Regions, Genetic / Q000502:physiology*; D012097:Repressor Proteins / Q000378:metabolism*; D014764:Viral Proteins / Q000378:metabolism
D001426:Bacterial Proteins; D004279:DNA, Viral; D004268:DNA-Binding Proteins; D034982:Integration Host Factors; D012097:Repressor Proteins; D014764:Viral Proteins; D003850:Deoxyribonuclease I