Biomedical subjects
Publications and source records attributed to C O Pabo.
The repressor of bacteriophage lambda is a protein containing two domains of approximately equal size. Fragments containing the amino-terminal domain of repressor bind specifically to lambda operator DNA and mediate positive and negative control of lambda transcription both in vitro and in vivo.
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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