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RING fingers mediate ubiquitin-conjugating enzyme (E2)-dependent ubiquitination.

A RING finger-containing protein (AO7) that binds ubiquitin-conjugating enzymes (E2s) and is a substrate for E2-dependent ubiquitination was identified. Mutations of cation-coordinating residues within AO7's RING finger abolished ubiquitination, as did chelation of zinc. Several otherwise-unrelated RING finger proteins, including BRCA1, Siah-1, TRC8, NF-X1, kf-1, and Praja1, were assessed for their ability to facilitate E2-dependent ubiquitination. In all cases, ubiquitination was observed. The RING fingers were implicated directly in this activity through mutations of metal-coordinating residues or chelation of zinc. These findings suggest that a large number of RING finger-containing proteins, with otherwise diverse structures and functions, may play previously unappreciated roles in modulating protein levels via ubiquitination.

Pubmed ID: 10500182


  • Lorick KL
  • Jensen JP
  • Fang S
  • Ong AM
  • Hatakeyama S
  • Weissman AM


Proceedings of the National Academy of Sciences of the United States of America

Publication Data

September 28, 1999

Associated Grants


Mesh Terms

  • Amino Acid Sequence
  • Ligases
  • Molecular Sequence Data
  • Ubiquitin-Conjugating Enzymes
  • Ubiquitins
  • Zinc
  • Zinc Fingers