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. 1973 Apr;70(4):1078–1082. doi: 10.1073/pnas.70.4.1078

Regulation by N Gene Protein of Phage Lambda of Anthranilate Synthetase Synthesis In Vitro

Robert P Dottin 1, Mark L Pearson 1
PMCID: PMC433429  PMID: 4515605

Abstract

The N protein of bacteriophage lambda is a positive regulator of early λ gene expression. In a λtrp transducing phage, λtrp46Nam, the synthesis of trp enzymes in vivo is also dependent on the presence of active N protein. The DNA of this phage has been used in a protein-synthesizing system in vitro to develop a biochemical assay for the activity of the N protein. From the following observations it appears that it is the N protein itself that stimulates trp enzyme synthesis in vitro. An activity that stimulates trp enzyme synthesis can be made in vitro by λN+ DNA but not by λNam DNA. This activity can also be detected in extracts of induced λN+ lysogens but not of λNam lysogens. Furthermore, the activity is temperature sensitive in similar extracts of λNts lysogens. No such activity is detectable in extracts of induced lysogens of λimm21. This phage makes all λ-coded gene products outside the immunity region, but lacks an N protein activity able to substitute for Nλ protein in vivo. Our experiments also show that the action of N protein is inhibited by the cI repressor protein in vivo as it is in vivo.

Keywords: N protein assay, temperature-sensitive N mutant protein, Nλ and N21 specificity, λ repressor

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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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