When proteins change partners

Saturday, September 12, 2009 - 07:35 in Biology & Nature

Dieter Wolf and colleagues at Burnham Institute for Medical Research (Burnham) have illuminated how competition between proteins enhances combinatorial diversity during ubiquitination (the process that marks proteins for destruction). Using S. pombe fission yeast as a model, the Wolf laboratory uncovered an intricate relationship, in which an array of Fbox proteins alternately attach to and are kicked off of a cullin-RING ubiquitin ligase (CRL1) containing CUL1 and Skp1. Without the Fbox, CRL1 cannot attach to the protein substrate or recruit ubiquitin, potentially preserving aberrant proteins. The research was published in the journal Molecular Cell on 11 September...

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