TY - JOUR
T1 - RFP is a DNA binding protein associated with the nuclear matrix
AU - Isomura, Takeshi
AU - Tamiya-koizumi, Keiko
AU - Suzuki, Motoshi
AU - Yoshida, Shonen
AU - Taniguchi, Masahiko
AU - Matsuyama, Mutsushi
AU - Ishigaki, Takeo
AU - Sakuma, Sadayuki
AU - Takahashi, Masahide
N1 - Funding Information:
This research was supported in part by a grant-in-aid for cancer research from the Ministry of Education, Science and Culture of Japan.
PY - 1992/10/25
Y1 - 1992/10/25
N2 - 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.
AB - 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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U2 - 10.1093/nar/20.20.5305
DO - 10.1093/nar/20.20.5305
M3 - Article
C2 - 1437549
AN - SCOPUS:0026661134
SN - 0305-1048
VL - 20
SP - 5305
EP - 5310
JO - Nucleic acids research
JF - Nucleic acids research
IS - 20
ER -