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Dimerization of the UmuD' protein in solution and its implications for regulation of SOS mutagenesis

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NMR spectroscopy has been used to determine that the dimerization interface of UmuD' in solution is not the homodimer interface originally inferred from crystallographic data. Instead, it resembles an interface that had been hypothesized to be involved in filamentation.

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Authors and Affiliations

  1. Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts, 02115, USA

    Ann E. Ferentz & Gerhard Wagner

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

    Timothy Opperman & Graham C. Walker

Authors
  1. Ann E. Ferentz
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  2. Timothy Opperman
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  3. Graham C. Walker
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  4. Gerhard Wagner
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Ferentz, A., Opperman, T., Walker, G. et al. Dimerization of the UmuD' protein in solution and its implications for regulation of SOS mutagenesis. Nat Struct Mol Biol 4, 979–982 (1997). https://doi.org/10.1038/nsb1297-979

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  • DOI: https://doi.org/10.1038/nsb1297-979

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