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A potentially life-saving protein takes shape
Date:7/2/2013

done in a test tube and uses x-ray crystallography to map the structures. Fushman's lab uses a different method that he says produces an environment somewhat closer to nature. The team used nuclear magnetic resonance spectroscopy (NMR) and other techniques to map the Lysine-11-linked chains.

The researchers found these chains take on a different shape in solution than in crystals, and are more flexible than was previously thought. Ubiquitin chains linked via Lysine-11 can form various three-dimensional shapes, and as salt concentrations change, the chains' shape also changes, the team found.

Researcher Carlos Castaeda and others in the Fushman lab reported their results in a paper published July 2 in the biological journal Structure.

The most-studied ubiquitin chain, linked via Lysine-48, is known as a "protein destroyer" because it labels cellular proteins to be broken up for later recycling. The UMD team found the cellular receptors responsible for breaking down proteins interact with Lysine-11 chains, but not as efficiently as with Lysine-48 chains. Therefore protein destruction does not appear to be the main task of the Lysine-11 linked chain, Fushman says; its function is something different and perhaps equally vital to maintaining healthy cells.


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Contact: Heather Dewar
hdewar@umd.edu
301-405-9267
University of Maryland
Source:Eurekalert

Page: 1 2

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