Open AccessA repressor heterodimer binds to a chimeric operator.
Author(s) -
Michael Hollis,
Dario Valenzuela,
David Pioli,
Robert H. Wharton,
Mark Ptashne
Publication year - 1988
Publication title -
proceedings of the national academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.85.16.5834
Subject(s) - repressor , operator (biology) , dna , chemistry , dna binding protein , stereochemistry , biology , gene , biochemistry , transcription factor
Replacement of the solvent-exposed residues of the DNA recognition helix of the 434 repressor with the corresponding residues of the P22 repressor generates a hybrid protein, 434R[alpha 3(P22R)], which binds specifically to P22 operators. We show here that a new DNA-binding specificity is generated by combining 434 and 434R[alpha 3(P22R)] repressor monomers to form a heterodimer. The heterodimer specifically recognizes a chimeric P22/434 operator that lacks two-fold rotational symmetry.
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