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Originally published In Press as doi:10.1074/jbc.M009298200 on November 21, 2000

J. Biol. Chem., Vol. 276, Issue 13, 10185-10190, March 30, 2001
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The Structure of the C4C4 RING Finger of Human NOT4 Reveals Features Distinct from Those of C3HC4 RING Fingers*

Hiroyuki HanzawaDagger §, Marjolein J. de Ruwe||**, Thomas K. Albert||Dagger Dagger , Peter C. van der Vliet||, H. T. Marc Timmers||§§, and Rolf BoelensDagger ¶¶

From the Dagger  Bijvoet Center for Biomolecular Research, Utrecht University, Padualaan 8, 3584 CH Utrecht, The Netherlands, the § Biomedical Research Laboratories, Sankyo, Limited, 2-58 Hiromachi 1-chome, Shinagawa-ku, Tokyo 140, Japan, and the || Laboratory for Physiological Chemistry and the Centre for Biomedical Genetics, University Medical Center Utrecht, 3508 AB Utrecht, The Netherlands

The NOT4 protein is a component of the CCR4·NOT complex, a global regulator of RNA polymerase II transcription. Human NOT4 (hNOT4) contains a RING finger motif of the C4C4 type. We expressed and purified the N-terminal region of hNOT4 (residues 1-78) encompassing the RING finger motif and determined the solution structure by heteronuclear NMR. NMR experiments using a 113Cd-substituted hNOT4 RING finger showed that two metal ions are bound through cysteine residues in a cross-brace manner. The three-dimensional structure of the hNOT4 RING finger was refined with root mean square deviation values of 0.58 ± 0.13 Å for the backbone atoms and 1.08 ± 0.12 Å for heavy atoms. The hNOT4 RING finger consists of an alpha -helix and three long loops that are stabilized by zinc coordination. The overall folding of the hNOT4 RING finger is similar to that of the C3HC4 RING fingers. The relative orientation of the two zinc-chelating loops and the alpha -helix is well conserved. However, for the other regions, the secondary structural elements are distinct.

* This work was supported in part by grants from the European Communities Program "Access to Large Scale Facilities" and by the Netherlands Foundation for Chemical Research.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.

The atomic coordinates and the structure factors (code 1E4U) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

The first two authors contributed equally to this work.

** Supported by the Dutch Cancer Foundation.

Dagger Dagger Supported by a postdoctoral fellowship from the Netherlands Organization for Scientific Research-Medical Sciences.

§§ Supported by a Pioneer grant from the Netherlands Organization for Scientific Research-Medical Sciences.

¶¶ To whom correspondence should be addressed. Tel.: 31-30-253-4035; Fax: 31-30-243-7623; E-mail: Boelens@NMR.chem.uu.nl.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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