In the polarity suppressor strain psuA 1, we observe a partial N independence of both transcription and DNA-membrane attachment for a lambda NN mutant. These results, in agreement with the genetical data reported by Dambly et al. (1976), suggest that the N product and rho factor are involved in the
Structure and function of mutants in the P gene of bacteriophage λ leading to the π phenotype
✍ Scribed by Reiser, Walter ;Leibrecht, Iris ;Klein, Albrecht
- Publisher
- Springer
- Year
- 1983
- Tongue
- English
- Weight
- 609 KB
- Volume
- 192
- Category
- Article
- ISSN
- 0026-8925
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✦ Synopsis
The location of 14 independently isolated spontaneous pi A and pi B point mutants in the lambda P gene and their base exchanges were determined. It was found that the pi B mutation is one unique type mapping close to other pi A mutants. The number of possible pi A mutation sites could be estimated. The mutation sites are distributed asymmetrically in the gene. The N-terminal half of the protein is unchanged. It is assumed to be required for the interaction with the lambda O protein. The P protein can be changed by substitution of a limited number of amino acids at the C-terminus. All functional proteins of this type have pi character. pi proteins do not appear to have altered intracellular levels or stabilities as compared to wild-type P protein. The plating characteristics of our mutants on two groP- mutants located in the dnaJ and dnaK genes, respectively, are strikingly different.
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