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Originally published In Press as doi:10.1074/jbc.M907300199 on March 13, 2000
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J Biol Chem, Vol. 275, Issue 20, 15432-15439, May 19, 2000

The Conserved RING-H2 Finger of ROC1 Is Required for Ubiquitin Ligation*

Angus ChenDagger , Kenneth Wu, Serge Y. Fuchs, Peilin Tan§, Carlos Gomez, and Zhen-Qiang Pan

From the Derald H. Ruttenberg Cancer Center, The Mount Sinai School of Medicine, New York, New York 10029-6574

ROC1 is a common component of a large family of ubiquitin E3 ligases that regulate cell cycle progression and signal transduction pathways. Here we present evidence suggesting that a conserved RING-H2 structure within ROC1 is critical for its ubiquitin ligation function. Mercury-containing sulfhydryl modification agents (rho -hydroxymercuribenzoate and mercuric chloride) irreversibly inhibit the ROC1-CUL1 ubiquitin ligase activity without disrupting the complex. Consistent with this, these reagents also eliminate the ability of the Skp1-CUL1-HOS-ROC1 E3 ligase complex to support the ubiquitination of Ikappa Balpha . Site-directed mutagenesis analysis identifies RING-H2 finger residues Cys42, Cys45, Cys75, His77, His80, Cys83, Cys94, and Asp97 as being essential for the ROC1-dependent ubiquitin ligase activity. Furthermore, C42S/C45S and H80A mutations reduce the ability of ROC1 to interact with CUL1 in transfected cells and diminish the capacity of ROC1-CUL1 to form a stable complex with Cdc34 in vitro. However, C75S, H77A, C94S, and D97A substitutions have no detectable effect on ROC1 binding activities. Thus, the ROC1 RING-H2 finger may possess multiple biochemical properties that include stabilizing an interaction with CUL1 and recruiting Cdc34. A possible role of the RING finger in facilitating the Ub transfer reaction is discussed.

* This work was supported by Public Health Service Grant GM55059 (to Z-Q. P.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger Supported in part by a National Institutes of Health predoctoral training grant in cancer biology.

§ Supported by a grant from the Peter Sharp Foundation.

Supported by the Life and Health Insurance Medical Research Fund, the New York Community Trust, and the Irma T. Hirschl Award. To whom correspondence should be addressed. Tel.: 212-659-5500; Fax: 212-849-2446; E-mail: ZQ_Pan@SMTPlink.mssm.edu.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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