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Vol. 10, Issue 8, 2595-2605, August 1999
§ and
*Laboratory of Molecular Biology, Department of Molecular and Cell
Biology, Division of Life Science, Graduate School of Agricultural
Science, Tohoku University, Sendai 981-8555, Japan;
Act3p/Arp4, an essential actin-related protein of
Saccharomyces cerevisiae located within the nucleus, is,
according to genetic data, involved in transcriptional regulation. In
addition to the basal core structure of the actin family members, which
is responsible for ATPase activity, Act3p possesses two insertions,
insertions I and II, the latter of which is predicted to form a
loop-like structure protruding from beyond the surface of the molecule. Because Act3p is a constituent of chromatin but itself does not bind to
DNA, we hypothesized that insertion II might be responsible for an
Act3p-specific function through its interaction with some other
chromatin protein. Far Western blot and two-hybrid analyses revealed
the ability of insertion II to bind to each of the core histones,
although with somewhat different affinities. Together with our finding
of coimmunoprecipitation of Act3p with histone H2A, this suggests the
in vivo existence of a protein complex required for correct expression
of particular genes. We also show that a conditional
act3 mutation affects chromatin structure of an episomal
DNA molecule, indicating that the putative Act3p complex may be
involved in the establishment, remodeling, or maintenance of chromatin structures.
Division of Molecular Biology and Genetics, Department
of Oncological Science, Huntsman Cancer Institute, University of Utah
Health Science Center, Salt Lake City, Utah 84132; and
Department of Molecular Genetics, Institute of Tumor
Biology and Cancer Research, University of Vienna, A-1090 Vienna,
Austria
Corresponding author. E-mail address:
mharata{at}biochem.tohoku.ac.jp.
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