Abstract
Plasmids were constructed to supply cII-coded protein for activation of the phage promoter p1. Using a fusion which expresses lacZ from p1, we can accurately follow activation of p1 without having to assay int activity in vivo. A large excess of cII protein compared to a normal lytic infection stimulates lacZ expression about 10-fold over the basal level. The int-c226 constitutive allele of p1 is not further activated by cII even though its level of lacZ expression is less than the maximal cII-activated expression from wild type p1. A himA-deleted strain also shows activation, demonstrating that there is no absolute requirement for the himA gene product for ell-stimulated transcription at pI.
| Original language | English |
|---|---|
| Pages (from-to) | 303-311 |
| Number of pages | 9 |
| Journal | Gene |
| Volume | 19 |
| Issue number | 3 |
| DOIs | |
| Publication status | Published - Oct 1982 |
| Externally published | Yes |
Keywords
- E. coli phage
- Gene cloning
- deletions
- hydroxylamine mutagenesis of plasmids
- recombinant DNA
- trp-lac fusions