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J Bacteriol. 1979 November; 140(2): 369-376

Cyclic adenosine 3',5'-monophosphate regulation of the bacteriophage T6/colicin K receptor in Escherichia coli.

ABSTRACT

Mutant strains of Escherichia coli unable to synthesize cyclic adenosine 3',5'-monophosphate (cAMP) or the cyclic adenosine monophosphate receptor protein (CRP) were more resistant than wild-type cells to infection by bacteriophage T6. This resistance was found to be associated with the decreased production of specific T6 receptor protein (also the colicin K receptor) located in the outer membrane protein fraction of these cells. Transcription of this particular outer membrane protein was regulated by the cAMP-CRP complex. A novel affinity technique coupled with sodium dodecyl sulfate-polyacrylamide gel electrophoresis was used in these investigations.