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A Bacteriophage Repressor/Operator Complex at 7 Å Resolution

  • S. C. Harrison
  • J. E. Anderson
Part of the NATO ASI Series book series (NSSA, volume 126)

Abstract

Possible mechanisms for sequence-specific affinity of proteins for DNA include: (1) ‘direct readout’ of base sequence by interactions of residues in the protein with functional groups on the DNA bases; (2) ‘indirect readout’ by interactions with backbone conformations sensitive to base sequence; (3) dependence of binding on long-range structural characteristics of DNA — e.g. twist, bend, or superhelicity; (4) induction of cooperative transitions in DNA, such as B -> A or B -> Z. The crystal structure of a bacteriophage repressor/operator complex, determined at 7 Å resolution, permits us to examine these mechanisms in the context of a particular example (Anderson et al·, 1985). The protein in this complex is the amino-terminal domain (residues 1-69 and denoted Rl-69) of the repressor encoded by coliphage 434, a close relative of bacteriophage λ. The DNA is a 14 base-pair synthetic oligonucleotide, with a self-complementary sequence (Fig. 1) that contains a consensus of the six repressor binding sites (operators) in the phage.

Keywords

Base Sequence Major Groove Backbone Conformation Cooperative Transition Direct Readout 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer Science+Business Media New York 1987

Authors and Affiliations

  • S. C. Harrison
    • 1
  • J. E. Anderson
    • 1
  1. 1.Department of Biochemistry and Molecular BiologyHarvard UniversityCambridgeUSA

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