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Nucleic Acids Research, 1992, Vol. 20, No. 20 5305-5310
© 1992


MOLECULAR BIOLOGY

RFP is a DNA binding protein associated with the nuclear matrix

Takeshi Isomura1,2, Keiko Tamiya-Koizumi3, Motoshi Suzuki3, Shonen Yoshida3, Masahiko Taniguchi1, Mutsushi Matsuyama1, Takeo Ishigaki2, Sadayuki Sakuma2 and Masahide Takahashi1,*

1Department of Pathology, Nagoya University School of Medicine 65 Tsurumai-cho, Showa-ku, Nagoya 466, Japan 2Department of Radiology, Nagoya University School of Medicine 65 Tsurumai-cho, Showa-ku, Nagoya 466, Japan 3Research Institute for Disease Mechanism and Control, Nagoya University School of Medicine 65 Tsurumai-cho, Showa-ku, Nagoya 466, Japan

* To whom correspondence should be addressed

Received July 24, 1992. Revised September 25, 1992. Accepted September 25, 1992.

We reported that the RFP gene encodes a protein with putative zinc finger domains and was involved In the activation of the ret proto-oncogene. To further characterize the RFP protein, we developed a polyclonal antibody against the product synthesized from a fragment of the RFP cDNA expressed in Escherichia coll. Western blot analysis showed that RFP was identified as a 58 kDa protein In cell lysates from four human and rodent cell lines and from mouse test is. In addition, a unique 68 kDa protein was detected in the testis. Using AH7974 (rat ascites hepatoma) and Raji (human Burkttt lymphoma) cells, we demonstrated strong association of RFP with the nuclear matrix. Furthermore, RFP solubilized from the nuclear matrix had DNA-bindlng activity although It appears to bind more preferentially to double-stranded DNA than to single-stranded DNA. These results thus suggest that RFP may play a role in molecular processes which occur in the nuclear matrix.


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