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

Author

Listed:
  • 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)

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.

Suggested Citation

  • Wei Li & Daqi Tu & Axel T. Brunger & Yihong Ye, 2007. "A ubiquitin ligase transfers preformed polyubiquitin chains from a conjugating enzyme to a substrate," Nature, Nature, vol. 446(7133), pages 333-337, March.
  • Handle: RePEc:nat:nature:v:446:y:2007:i:7133:d:10.1038_nature05542
    DOI: 10.1038/nature05542
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