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Association of protein kinase CK2 with nuclear matrix: Influence of method of preparation of nuclear matrix
Author(s) -
Tawfic Sherif,
Davis Alan T.,
Faust Russell A.,
Gapany Markus,
Ahmed Khalil
Publication year - 1997
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/(sici)1097-4644(19970301)64:3<499::aid-jcb16>3.0.co;2-b
Subject(s) - nuclear matrix , chromatin , cytoskeleton , cytosol , microbiology and biotechnology , cell nucleus , nuclear protein , biophysics , biology , enzyme , nucleus , chemistry , biochemistry , transcription factor , cell , dna , gene
Nuclear matrix (NM) plays roles of fundamental structural and functional significance as the site of replication, transcription, and RNA processing and transport, acting as an anchor or attachment site for a variety of enzymes and other proteins involved in these activities. We have previously documented that protein kinase CK2 translocates from the cytosol to the nucleus, where it associates preferentially with chromatin and NM, in response to certain growth stimuli. Considering that characteristics of the isolated NM can depend on the procedure employed for its isolation, we compared three standard methods for NM preparation to confirm the association of intrinsic CK2 with this structure. Our data suggest that the method used for isolating the NM can quantitatively influence the measurable NM‐associated CK2. However, all three methods employed yielded qualitatively similar results with respect to the stimulus‐mediated modulation of NM‐associated CK2, thus further supporting the notion that NM is an important site for physiologically relevant functions of CK2. In addition, core filaments and cytoskeleton that were isolated by two of the preparative methods had a small but significant level of associated CK2 activity. J. Cell. Biochem. 64:499–504. © 1997 Wiley‐Liss, Inc. This article is a U.S. Government work and, as such, is in the public domain in the United States of America.