Soumillion, Patrice
[UCL]
Fastrez, Jacques
[UCL]
The R gene coding for phage lambda lysozyme (lambda L), cloned under the control of the PL promoter on a multicopy vector, is expressed in an Escherichia coli strain auxotrophic for tryptophan. Induction by a thermal shift after tryptophan supplementation in a culture initially brought into stationary phase by tryptophan starvation leads to highly increased expression. A thermally unstable mutant protein, difficult to obtain under standard conditions, can be easily produced by post-stationary-phase expression. It is shown that this is due to a drastic decrease in the heat-shock-induced proteolysis normally observed on thermal induction. These data are discussed in relation to our present knowledge of stringent and heat-shock responses.
Bibliographic reference |
Soumillion, Patrice ; Fastrez, Jacques. A large decrease in heat-shock-induced proteolysis after tryptophan starvation leads to increased expression of phage lambda lysozyme cloned in Escherichia coli.. In: The Biochemical journal, Vol. 286 ( Pt 1), p. 187-91 (1992) |
Permanent URL |
http://hdl.handle.net/2078.1/9609 |