Dual E1 activation systems for ubiquitin differentially regulate E2 enzyme charging

Jianping Jin, Xue Li, Steven P. Gygi and J. Wade Harper ()
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Jianping Jin: Harvard Medical School, 77 Avenue Louis Pasteur, Boston, Massachusetts 02115, USA
Xue Li: Harvard Medical School, 200 Longwood Drive, Boston, Massachusetts 02115, USA
Steven P. Gygi: Harvard Medical School, 200 Longwood Drive, Boston, Massachusetts 02115, USA
J. Wade Harper: Harvard Medical School, 77 Avenue Louis Pasteur, Boston, Massachusetts 02115, USA

Nature, 2007, vol. 447, issue 7148, 1135-1138

Abstract: A divergent E1 in vertebrates and sea urchin, Uba6, is identified, which specifically activates ubiquitin but not other ubiquitin-like proteins in vitro and in vivo. Human Uba6 and Ube1 have distinct preferences for E2 charging in vitro, and their specificity depends in part on their C-terminal ubiquitin-fold domains, which recruit E2s.

Date: 2007
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DOI: 10.1038/nature05902

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