期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1979
卷号：76
期号：4
页码：1608-1612
DOI：10.1073/pnas.76.4.1608
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：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.
