Abstract
The amount of tryptophanase was estimated in Escherichia coli deltadnaJ and deltadnaKdnaJ mutants. Densitometric analysis of polyacrylamide gels demonstrated that the amount of tryptophanase was diminished in both mutants. DnaK and DnaJ molecular chaperones apparently influence the amount of tryptophanase, the expression of which is regulated at all transcription steps, including transcription elongation. The half-life of GreA and GreB proteins (being activators of transcription elongation of the tna operon) are diminished in both mutants suggesting the involvement of DnaK and DnaJ in the stability of these proteins.
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