| Literature DB >> 3413061 |
M Hollis1, D Valenzuela, D Pioli, R Wharton, M Ptashne.
Abstract
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.Entities:
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Year: 1988 PMID: 3413061 PMCID: PMC281859 DOI: 10.1073/pnas.85.16.5834
Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN: 0027-8424 Impact factor: 11.205