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. 1979 Apr;76(4):1608–1612. doi: 10.1073/pnas.76.4.1608

The lambda repressor contains two domains.

C O Pabo, R T Sauer, J M Sturtevant, M Ptashne
PMCID: PMC383439  PMID: 287002

Abstract

Papain digestion of the lambda phage repressor produces two fragments that are relatively resistant to further digestion. One includes the amino terminus (residues 1-92) and the other the carboxyl terminus (residues 132-236). Calorimetry shows that the amino-terminal fragment denatures near 50 degrees C and that the carboxyl-terminal fragment denatures near 70 degrees C. Intact repressor undergoes two denaturations, one near 50 degrees C and another near 70 degrees C. These and other data show that lambda repressor consists of two domains joined by a "connector" 40 amino acids long that is sensitive to proteases. The amino-terminal domain binds DNA, and the carboxyl-terminal domain oligomerizes.

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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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