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J. Biol. Chem., Vol. 277, Issue 23, 20611-20617, June 7, 2002
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From the Department of Life Science, Graduate School and Faculty of
Science, Himeji Institute of Technology, Kamigori, Hyogo 678-1201, Japan
Using a monoclonal antibody that recognizes a
nuclear matrix protein, we selected a cDNA clone from a
The Newly Identified Human Nuclear Protein NXP-2 Possesses
Three Distinct Domains, the Nuclear Matrix-binding, RNA-binding, and
Coiled-coil Domains*
,
gt11
human placenta cDNA library. This cDNA encoded a 939-amino acid
protein designated nuclear matrix protein NXP-2. Northern blot analysis
indicated that NXP-2 was expressed in various tissues at different
levels. Forcibly expressed green fluorescent protein-tagged
NXP-2 as well as endogenous NXP-2 was localized in the nucleus and
distributed to the nuclear matrix. NXP-2 was released from the nuclear
matrix when RNase A was included in the buffer for nuclear matrix
preparation. Mapping of functional domains was carried out using green
fluorescent protein-tagged truncated mutants of NXP-2. The region of
amino acids 326-353 was responsible for nuclear matrix binding and
contained a cluster of hydrophobic amino acids that was similar to the
nuclear matrix targeting signal of acute myeloleukemia protein. The
central region (amino acids 500-591) was demonstrated to be required
for RNA binding by Northwestern analysis, although NXP-2 lacked a known
RNA binding motif. The region of amino acid residues 682-876 was
predicted to have a coiled-coil structure. The RNA-binding, nuclear matrix-binding, and coiled-coil domains are structurally separated, suggesting that NXP-2 plays important roles in diverse nuclear functions, including RNA metabolism and maintenance of nuclear architecture.
*
This work was supported in part by grants-in-aid from the
Ministry of Education, Science and Culture of Japan.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.
Present address: Dept. of Developmental Biology, National
Institute for Basic Biology, Myodaiji-cho, Okazaki 444-8585, Japan.
§
To whom correspondence should be addressed: Dept. of Life Science,
Himeji Institute of Technology 3-2-1 Koto, Kamigori-chou, Ako-gun,
678-1201 Japan. Tel.: 81-791-58-0434; Fax: 81-791-58-0193; E-mail:
sadano@sci.himeji-tech.ac.jp.
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