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Design of thermolabile bacteriophage repressor mutants by comparative molecular modeling

Nature Biotechnology volume 15, pages 980–983 (1997)Cite this article

Abstract

Comparative molecular modeling was performed with repressor protein Rro of the temperate Lactococcus lactis bacteriophage r1t using the known 3D-structures of related repressors in order to obtain thermolabile derivatives of Rro. Rro residues presumed to stabilize a nonhomologous but structurally conserved hydrophobic pocket, which was shown to be important for thermostability of the Escherichia coli bacteriophage lambda repressor Cl, were randomized. Of the derivatives that exhibited various temperature-sensitive phenotypes, one was shown to hold promise for both fundamental and industrial applications that require the controlled production of (heterologous) proteins in L. lactis.

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Author notes

  1. Gerard Venema: Corresponding author: (e-mail: g.venema@biol.rug.nl).

Authors and Affiliations

  1. Department of Genetics, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Kerklaan 30, 9751, NNHaren, The Netherlands

    Arjen Nauta, Bertus van den Burg, Harma Karsens & Jan Kok

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  1. Arjen Nauta
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  2. Bertus van den Burg
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  3. Harma Karsens
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  4. Gerard Venema
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  5. Jan Kok
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Nauta, A., Burg, B., Karsens, H. et al. Design of thermolabile bacteriophage repressor mutants by comparative molecular modeling. Nat Biotechnol 15, 980–983 (1997). https://doi.org/10.1038/nbt1097-980

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