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Originally published In Press as doi:10.1074/jbc.M011208200 on March 30, 2001

J. Biol. Chem., Vol. 276, Issue 26, 23992-23999, June 29, 2001
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A Novel Human Striated Muscle RING Zinc Finger Protein, SMRZ, Interacts with SMT3b via Its RING Domain*

Ken-Shwo DaiDagger and Choong-Chin Liew§

From the Institute of Medical Science and Department of Laboratory Medicine and Pathobiology, University of Toronto, Toronto, Ontario M5G 1L5, Canada

The RING domain is a conserved zinc finger motif, which serves as a protein-protein interaction interface. Searches of a human heart expressed sequence tag data base for genes encoding the RING domain identified a novel cDNA, named striated muscle RING zinc finger protein (SMRZ). The SMRZ cDNA is 1.9 kilobase pairs in length and encodes a polypeptide of 288 amino acid residues; analysis of the peptide sequence demonstrated an N-terminal RING domain. Fluorescence in situ hybridization localized SMRZ to chromosome 1p33-34. Northern blots demonstrated that SMRZ is expressed exclusively in striated muscle. In the cardiovascular system, SMRZ is more highly expressed in the fetal heart than in the adult heart (slightly higher expression in the ventricle than in the atrium), suggesting that SMRZ is developmentally regulated. SMRZ was found to interact with SMT3b, a ubiquitin-like protein, through the SMRZ-RING domain. This interaction was abolished by mutagenesis of conserved RING domain residues. Transient transfection of SMRZ into C2C12 myoblasts showed localization of SMRZ to the nucleus. These data suggest that SMRZ may play an important role in striated muscle cell embryonic development and perhaps in cell cycle regulation.


* This work was supported in part by the Medical Research Council of Canada, the Heart and Stroke Foundation of Ontario, and the Canadian Genome Analysis and Technology Program.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 Recipient of a Heart and Stroke Foundation traineeship.

§ To whom correspondence should be addressed: Cardiovascular Genome Unit, Brigham and Women's Hospital, Harvard Medical School, 75 Francis St., Thorn 1326, Boston, MA 02115. Tel.: 617-732-8117; Fax: 617-975-0995; E-mail: liewcc@tcgu.med.utoronto.ca.


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