The lambda repressor contains two domains.
- 1 April 1979
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 76 (4), 1608-1612
- https://doi.org/10.1073/pnas.76.4.1608
Abstract
Papain digestion of the .lambda. phage repressor produces 2 fragments that are relatively resistant to further digestion. One includes the amino [N] terminus (residues 1-92) and the other the C terminus (residues 132-236). Calorimetry shows that the N-terminal fragment denatures near 50.degree. C and that the C-terminal fragment denatures near 70.degree. C. Intact repressor undergoes 2 denaturations, one near 50.degree. C and another near 70.degree. C. These and other data show that .lambda. repressor consists of 2 domains joined by a connector 40 amino acids long that is sensitive to proteases. The N-terminal domain binds DNA, and the C-terminal domain oligomerizes.Keywords
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