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Biochemistry

Rear view of an enzyme

Nature volume 497, pages 576–577 (2013)Cite this article

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The enzyme Ubc9 mediates attachment of the small modifier protein SUMO to target proteins. It emerges that for optimal functioning — and for proper meiotic cell division — Ubc9 itself must be modified by SUMO.

Chemical modification can change a protein's fate and behaviour. One such modification is SUMOylation, which involves covalent attachment of the small protein SUMO to target proteins. SUMOylated proteins can carry individual SUMO molecules or chains, with each modification resulting in a different fate. Typically, the addition of SUMO chains through the process of polySUMOylation marks the target for further tagging with chains of the SUMO-related protein ubiquitin and so for degradation1. Writing in Molecular Cell, Klug et al.2 show that enhanced polySUMOylation is essential for meiotic cell division. The authors also describe how the balance is tipped between the addition of a single SUMO and a SUMO chainFootnote 1.

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Figure 1: Forging a link in the SUMO chain.

Notes

  1. *This News & Views article was published online on 22 May 2013.

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  1. Mary Dasso is in the Program in Cellular Regulation and Metabolism, National Institute of Child Health and Human Development, Bethesda, Maryland 20892, USA.

    Mary Dasso

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  1. Mary Dasso
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Correspondence to Mary Dasso.

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Dasso, M. Rear view of an enzyme. Nature 497, 576–577 (2013). https://doi.org/10.1038/nature12249

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