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Science 13 October 2000: Vol. 290. no. 5490, pp. 337 - 341 DOI: 10.1126/science.290.5490.337
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Reports
A Myosin I Isoform in the Nucleus
Lidija Pestic-Dragovich,1*
Ljuba Stojiljkovic,1*
Anatoly A. Philimonenko,2
Grzegorz Nowak,1
Yunbo Ke,1
Robert E. Settlage,3
Jeffrey Shabanowitz,3
Donald F. Hunt,4
Pavel Hozak,2
Primal de Lanerolle1
A nuclear isoform of myosin I that contains a unique 16-amino
acid amino-terminal extension has been identified. An affinity-purified antibody to the 16-amino acid peptide demonstrated nuclear staining. Confocal and electron microscopy revealed that nuclear myosin I colocalized with RNA polymerase II in an -amanitin- and actinomycin D-sensitive manner. The antibody coimmunoprecipitated RNA
polymerase II and blocked in vitro RNA synthesis. This isoform of
myosin I appears to be in a complex with RNA polymerase II and may affect transcription.
1 Department of Physiology and Biophysics,
University of Illinois at Chicago, Chicago, IL 60612, USA.
2 Department of Cell Ultrastructure and Molecular
Biology, Institute of Experimental Medicine, Academy of Sciences of the
Czech Republic, Prague, Czech Republic.
3 Chemistry
Department, University of Virginia, Charlottesville, VA 22901, USA.
4 Departments of Chemistry and Pathology, University
of Virginia, Charlottesville, VA 22901, USA.
*
These authors contributed equally to this paper.
To whom correspondence should be addressed. E-mail:
primal{at}uic.edu
Read the Full Text
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