Abstract
A deletion htpR mutant of Escherichia coli has been constructed on the basis of site-directed mutagenesis. To this end, the chromosomal allele of htpR gene was substituted by a mutant allele introduced into the cell with a recombinant plasmid. The htpR mutant is characterized by a reduced level of proteolysis and therefore by a decreased rate of proteolytic degradation of RNA polymerase of bacteriophage T7. The mutation in htpR is linked with chloramphenicol resistance.
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