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J. Biol. Chem., Vol. 277, Issue 44, 42259-42267, November 1, 2002
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From the Herman B Wells Center for Pediatric Research, Section of
Pediatric Hematology/Oncology, Department of Pediatrics and
Department of Biochemistry and Molecular Biology, Indiana
University School of Medicine, Indianapolis, Indiana 46202
CpG-binding protein (CGBP) binds unmethylated CpG
dinucleotides and is essential for mammalian development. CGBP exhibits a punctate nuclear localization correlated with
4,6-diamidino-2-phenylindole light regions and is excluded from
metaphase chromosomes. The distribution of CGBP is distinct from the
heterochromatin-associated proteins MBD1, methyl-CpG-binding protein 2, and HP1
CpG-binding Protein Is a Nuclear Matrix- and
Euchromatin-associated Protein Localized to Nuclear Speckles Containing
Human Trithorax
IDENTIFICATION OF NUCLEAR MATRIX TARGETING SIGNALS*
. Some CGBP-containing nuclear speckles co-localize with
splicing factor SC-35 and actively transcribed regions of the genome,
whereas most CGBP co-localizes with acetylated histones, indicating
that CGBP is localized to active chromatin. CGBP contains two nuclear
localization signals that are insufficient to direct punctate
subnuclear distribution. Instead, localization of CGBP to nuclear
speckles requires signals within the acidic, basic, and coiled-coil
domains. CGBP associates with the nuclear matrix, and fragments of CGBP
that fail to associate with the nuclear matrix fail to localize to
nuclear speckles and exhibit reduced transcriptional activation
activity. Mutated versions of CGBP that lack DNA binding activity
exhibit a normal nuclear distribution, suggesting that CGBP accumulates
at nuclear speckles as a result of protein/protein interactions.
Importantly, the subcellular distribution of CGBP is identical to human
trithorax, suggesting that these proteins may be components of a
multimeric complex analogous to the histone-methylating Set1 complex of
Saccharomyces cerevisiae that contains CGBP and trithorax homologues.
*
This work was supported by National Institutes of Health
Grant CA58947 (to D. G. S.) and by the Riley Memorial Association.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.
To whom correspondence should be addressed: Herman B Wells Center
for Pediatric Research, Cancer Research Bldg., Rm. 472, Indiana
University School of Medicine, 1044 W. Walnut St., Indianapolis, IN
46202. Tel.: 317-274-8977; Fax: 317-274-8928; E-mail:
dskalnik@iupui.edu.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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