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Homology among DNA-binding proteins suggests use of a conserved super-secondary structure

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Abstract

The amino acid sequences of the repressor and cro proteins of phages λ, 434 and P22 are homologous, especially in a region in which repressor and λ cro have a similar α-helix–turn–α-helix secondary structure. Model-building studies indicate that this structure is important in DNA binding, and we suggest it may be a common feature of many DNA-binding proteins.

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Authors and Affiliations

  1. Department of Biology, Massachusetts Institute of Technology, Cambridge, Massachusetts, 02139, USA

    R. T. Sauer

  2. Department of Biochemistry and Molecular Biology, Harvard University, Cambridge, Massachusetts, 02138, USA

    R. R. Yocum, M. Lewis & C. O. Pabo

  3. Department of Chemistry, University of California, San Diego, La Jolla, California, 92093, USA

    R. F. Doolittle

Authors
  1. R. T. Sauer
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  2. R. R. Yocum
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  3. R. F. Doolittle
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  4. M. Lewis
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  5. C. O. Pabo
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Sauer, R., Yocum, R., Doolittle, R. et al. Homology among DNA-binding proteins suggests use of a conserved super-secondary structure. Nature 298, 447–451 (1982). https://doi.org/10.1038/298447a0

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