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Enzyme mechanisms

What's up 'Doc'?

Nature Chemical Biology volume 9, pages 756–757 (2013)Cite this article

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An Erratum to this article was published on 17 January 2014

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The Doc-Phd pair forms a bacterial toxin-antitoxin system, but the mechanism by which the Fic-family member Doc causes toxicity is not fully defined. New research shows that Doc unexpectedly functions as a kinase to phosphorylate elongation factor TU, thus inhibiting translation and leading to Doc-mediated growth arrest.

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Figure 1: Doc phosphorylates EF-Tu to inhibit translation.

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  • 11 December 2013

    In the version of this article initially published, the citation to reference 4 incorrectly referred to 'Castro-Roa, K.'. The correct author's name is 'Castro-Roa, D.'. The error has been corrected in the HTML and PDF versions of the article.

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Authors and Affiliations

  1. Wolfgang Peti is at the Department of Molecular Pharmacology, Physiology and Biotechnology and at the Department of Chemistry, Brown University, Providence, Rhode Island, USA.,

    Wolfgang Peti

  2. Rebecca Page is at the Department of Molecular Biology, Cell Biology and Biochemistry, Brown University, Providence, Rhode Island, USA.,

    Rebecca Page

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  1. Wolfgang Peti
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  2. Rebecca Page
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Correspondence to Rebecca Page.

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The authors declare no competing financial interests.

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Peti, W., Page, R. What's up 'Doc'?. Nat Chem Biol 9, 756–757 (2013). https://doi.org/10.1038/nchembio.1379

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