A Repressor Heterodimer Binds to a Chimeric Operator

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[α 3(P22R)], which binds specifically to P22 operators. We show here that a new DNA-binding specificity is generated by c...

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Veröffentlicht in:	Proceedings of the National Academy of Sciences - PNAS 1988-08, Vol.85 (16), p.5834-5838
Hauptverfasser:	Hollis, Melvyn, Valenzuela, Dario, Pioli, David, Wharton, Robin, Ptashne, Mark
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino acids Base Sequence Biochemistry Chemicals industries Deoxyribonuclease I - pharmacology Dimers DNA Hybridity Monomers Mutagenesis Mutation Operator Regions, Genetic phage P22 Plasmids Repressor Proteins - metabolism Symmetry Transcription Factors - metabolism
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Beschreibung
Zusammenfassung:	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[α 3(P22R)], which binds specifically to P22 operators. We show here that a new DNA-binding specificity is generated by combining 434 and 434R[α 3(P22R)] repressor monomers to form a heterodimer. The heterodimer specifically recognizes a chimeric P22/434 operator that lacks two-fold rotational symmetry.
ISSN:	0027-8424 1091-6490
DOI:	10.1073/pnas.85.16.5834