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News and Views
Nature 445, 375-376 (25 January 2007) | doi:10.1038/nature05564; Published online 14 January 2007
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Postdoctoral Research Fellows
- Northwestern University
- Chicago, Illinois, United States
Post Doctoral Research Associate
- University of Illinois
- Urbana United States
Structural biology: Pass the protein
Jean-François Trempe1 & Jane A. Endicott1
Abstract
Modifier proteins, such as ubiquitin, are passed sequentially between trios of enzymes, like batons in a relay race. Crystal structures suggest the mechanism of transfer between the first two enzymes.
Proteins are essential for all cellular processes, but their activities must be tightly controlled. One way of doing this is to covalently attach a small protein such as ubiquitin, or other ubiquitin-like proteins (UBLs)1, 2 such as NEDD8 and SUMO.
- Jean-François Trempe and Jane A. Endicott are in the Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
Email: jane.endicott@biop.ox.ac.uk
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