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Cell biology

Phosphate on, rubbish out

Nature volume 539, pages 38–39 (2016)Cite this article

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A previously unknown way in which cells mark proteins for destruction has been found in bacteria — phosphorylation of the amino acid arginine targets proteins for degradation by protease enzymes. See Article p.48

Bacteria are expert at adapting to changing lifestyles. Dealing with damaged or misfolded proteins is a key challenge during adaptation to stressful conditions such as high temperature. In such situations, chaperone proteins restore unfolded proteins to their functional, folded states and protease enzymes degrade damaged proteins1. But how are proteins that have been damaged beyond redemption recognized and sent for degradation? On page 48, Trentini et al.2 show that a surprisingly simple degradation tag — phosphorylation of the amino acid arginine — has a central role in the handling of heat-damaged proteins in the bacterium Bacillus subtilis.

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Figure 1: Protein destruction by protease enzymes.

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References

  1. Wickner, S., Maurizi, M. R. & Gottesman, S. Science 286, 1888–1893 (1999).

    Article  CAS  Google Scholar 

  2. Trentini, D. B. et al. Nature 539, 48–53 (2016).

    Article  ADS  CAS  Google Scholar 

  3. Olivares, A. O., Baker, T. A. & Sauer, R. T. Nature Rev. Microbiol. 14, 33–44 (2015).

    Article  Google Scholar 

  4. Hershko, A. & Ciechanover, A. Annu. Rev. Biochem. 67, 425–479 (1998).

    Article  CAS  Google Scholar 

  5. Jastrab, J. B. & Darwin, K. H. Annu. Rev. Microbiol. 69, 109–127 (2015).

    Article  CAS  Google Scholar 

  6. Sauer, R. T. & Baker, T. A. Annu. Rev. Biochem. 80, 587–612 (2011).

    Article  CAS  Google Scholar 

  7. Neher, S. B., Flynn, J. M., Sauer, R. T. & Baker, T. A. Genes Dev. 17, 1084–1089 (2003).

    Article  CAS  Google Scholar 

  8. Krüger, E., Zühlke, D., Witt, E., Ludwig, H. & Hecker, M. EMBO J. 20, 852–863 (2001).

    Article  Google Scholar 

  9. Fuhrmann, J. et al. Science 324, 1323–1327 (2009).

    Article  ADS  CAS  Google Scholar 

  10. Schmidt, A. et al. Mol. Cell. Proteom. 13, 537–550 (2014).

    Article  CAS  Google Scholar 

  11. Elsholz, A. K., Michalik, S., Zühlke, D., Hecker, M. & Gerth, U. EMBO J. 29, 3621–3629 (2010).

    Article  CAS  Google Scholar 

  12. Kirstein, J., Dougan, D. A., Gerth, U., Hecker, M. & Turgay, K. EMBO J. 26, 2061–2070 (2007).

    Article  CAS  Google Scholar 

  13. Wozniak, D. J., Tiwari, K. B., Soufan, R. & Jayaswal, R. K. Microbiology 158, 2568–2576 (2012).

    Article  CAS  Google Scholar 

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Authors and Affiliations

  1. Arti Tripathi and Susan Gottesman are in the Laboratory of Molecular Biology, National Cancer Institute, Bethesda, Maryland 20892, USA.,

    Arti Tripathi & Susan Gottesman

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  1. Arti Tripathi
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  2. Susan Gottesman
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Correspondence to Susan Gottesman.

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Tripathi, A., Gottesman, S. Phosphate on, rubbish out. Nature 539, 38–39 (2016). https://doi.org/10.1038/539038a

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