A ubiquitin ligase transfers preformed polyubiquitin chains from a conjugating enzyme to a substrate

Wei Li, Daqi Tu, Axel T. Brunger and Yihong Ye ()
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Wei Li: Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA
Daqi Tu: The Howard Hughes Medical Institute, Neurology and Neurological Sciences, Structural Biology, and SSRL, Stanford University, Stanford, California 94305-5489, USA
Axel T. Brunger: The Howard Hughes Medical Institute, Neurology and Neurological Sciences, Structural Biology, and SSRL, Stanford University, Stanford, California 94305-5489, USA
Yihong Ye: Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA

Nature, 2007, vol. 446, issue 7133, 333-337

Abstract: It is demonstrated that polyubiquitination mediated by Ube2g2 (E2) and gp78 (E3) employs a mechanism that involves preassembly of Lys48-linked ubiquitin chains at the catalytic cysteine of Ube2g2. Polyubiquitination of a substrate can be achieved by transferring the preassembled ubiquitin chains from Ube2g2 to a lysine residue in a substrate.

Date: 2007
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DOI: 10.1038/nature05542

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