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Perturbation of lac Operator DNA Modification by Tryptic Core Protein from lac Repressor
Susan P. Manly, George N. Bennett and Kathleen Shive Matthews
Proceedings of the National Academy of Sciences of the United States of America
Vol. 80, No. 20, [Part 1: Biological Sciences] (Oct. 15, 1983), pp. 6219-6223
Published by: National Academy of Sciences
Stable URL: http://www.jstor.org/stable/23030
Page Count: 5
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Operator DNA fragments were modified in the presence of lac repressor protein or its trypsin-resistant core. Operator DNA was alkylated or cleaved enzymatically with these related proteins present to compare the influences of their binding on the reactivities or enzymatic susceptibilities of individual bases in the sequence. These two protein species have pronounced and distinguishable effects on the reactivity of the bases of the operator fragment toward methylation by dimethyl sulfate. Perturbation of base alkylation by the trypsin-resistant core repressor is most pronounced in the inner, asymmetric region of the operator DNA, while repressor effects extend further on either end of the operator sequence. Digestion of the two protein-operator complexes by DNase I yields fragment patterns that differ primarily in extent of protection. These data extend the experimental base supporting the involvement of the core region of the lac repressor in addition to its NH2 termini in the operator-specific binding activity of this protein.
Proceedings of the National Academy of Sciences of the United States of America © 1983 National Academy of Sciences