Summary
In the rho-15 temperature-sensitive (ts) mutant deo−operon enzymes show no sensitivity to catabolite repression and are not derepressed under the influence of a constitutive regulatory mutation, cytR. These data suggest that intact Rho-protein along with CRP protein is necessary for a catabolite sensitive deo−operon promoter cytP to work. In addition, there are data suggesting that Rho-factor and CRP-protein interact with each other in regulation of the deo−operon. Thus, in studies of the effect of the rho-15 (ts) and crp mutations, maximum deo−enzyme levels have been found in the double rho-15 (ts) crp mutant, and therefore intact Rho-protein in the crp genome or intact CRP-protein on the rho-15 (ts) background seems to be an obstacle for the deoP promoter in the deo-operon. In rho-15 (ts) a relative increase has been observed in the enzyme activity for a distal purine nucleoside phosphorylase gene with respect to a proximal thymidine phosphorylase gene. However in crp, the rho-15 (ts) mutation has no effect on the polarity gradient, that is on the background of impaired CRP protein Rho-factor does not seem to work as a transcription terminator within the operon.
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Communicated by G. O'Donovan
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Sukhodolets, V.V., Mironov, A.S. & Linkova, E.V. Influence of the rho-15 temperature-sensitive (ts) mutation on the expression of the deo−operon in Escherichia coli . Molec. Gen. Genet. 187, 157–161 (1982). https://doi.org/10.1007/BF00384399
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DOI: https://doi.org/10.1007/BF00384399