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Volume 272, Number 27, Issue of July 4, 1997 pp. 17176-17181
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

Evidence for the Presence of Myosin I in the Nucleus

(Received for publication, February 26, 1997, and in revised form, April 30, 1997)

Grzegorz Nowak , Lidija Pestic-Dragovich , Pavel Hozák ^¶ , Anatoly Philimonenko ^¶ , Cal Simerly , Gerald Schatten and Primal de Lanerolle

From the  Department of Physiology and Biophysics, University of Illinois, Chicago, Illinois 60612-7246, the ^¶ Department of Cell Ultrastructure and Molecular Biology, Institute of Experimental Medicine, Videnska 1083, 14220 Prague 4, Czech Republic, and the  Departments of Zoology and Obstetrics & Gynecology, University of Wisconsin, Madison, Wisconsin 53706

We produced and affinity-purified polyclonal antibodies to adrenal myosin I. These antibodies recognize adrenal myosin I by Western blot analysis (116 kDa) and inhibit the actin-activated ATPase activity of purified adrenal myosin I. They also recognize a 120-kDa protein in extracts prepared from many different cell lines. Fluorescence microscopy demonstrated the presence of immunoreactive material in the perinuclear region, the leading edges, and the nuclei of 3T3 cells. Fluorescence microscopy also demonstrated nuclear staining in mouse oocytes at the germinal vesicle stage and in the pronuclei during fertilization. Confocal and immunoelectron microscopy confirmed the intranuclear localization. Electron microscopy also demonstrated staining of structures in nucleoli that are thought to be associated with rDNA transcription. Western blot analyses revealed the presence of the 120-kDa protein in extracts prepared from nuclei that are apparently free of cytosolic contamination. The same nuclear protein binds ¹²⁵I-calmodulin and is photoaffinity labeled with [-³²P]ATP. The 120-kDa protein was partially purified from twice washed nuclei using ammonium sulfate fractionation and gel filtration chromatography. Column fractions containing 120-kDa protein as revealed by Western blot analysis also contain K⁺-EDTA ATPase activity. The 120-kDa protein was also shown to bind actin in the absence, but not the presence, of ATP. Since K⁺-EDTA ATPase activity, actin, and ATP binding are defining features of the members of the myosin superfamily of proteins, we propose that the 120-kDa protein is a previously undescribed myosin I isoform that is an intranuclear actin-based molecular motor.

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