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. 1984 Jul;159(1):238–242. doi: 10.1128/jb.159.1.238-242.1984

Control of bacteriophage lambda CII activity by bacteriophage and host functions.

A Rattray, S Altuvia, G Mahajna, A B Oppenheim, M Gottesman
PMCID: PMC215619  PMID: 6330032

Abstract

We have studied the regulation of the lambda cII gene in vivo using cloned lambda fragments. Lambda N protein stimulated cII expression. Surprisingly, although very high cII protein levels were detected by gel electrophoresis, little cII protein activity, measured as stimulation of the lambda pI and pE promoters, was observed. The half-life of cII protein depended critically on its initial level. At low concentrations its half-life was as short as 1.5 min, whereas at high cII protein levels, it could be as long as 22 min. The Escherichia coli mutant ER437 directs lambda towards lysogeny; cII protein was more stable in this strain than in the wild type. On the other hand, although cyclic AMP is required for efficient lysogeny, it did not appear to influence the synthesis, stability, or activity of cII protein.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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