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Proc Natl Acad Sci U S A. 1999 Sep 28;96(20):11364-9.

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

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  • 1Laboratory of Immune Cell Biology, Division of Basic Sciences, National Cancer Institute, Building 10, Room 1B34, National Institutes of Health, 9000 Rockville Pike, Bethesda, MD 20892-1152, USA.

Abstract

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.

PMID:
10500182
[PubMed - indexed for MEDLINE]
PMCID:
PMC18039
Free PMC Article

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