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Nuclear estrogen receptor II (nER‐II) is involved in the estrogen‐dependent ribonucleoprotein transport in the goat uterus: II. isolation and characterization of three small nuclear ribonucleoprotein proteins which bind to nER‐II
Author(s) -
Sebastian Thomas,
Thampan Raghava Varman
Publication year - 2001
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/jcb.1280
Subject(s) - ribonucleoprotein , small nuclear ribonucleoprotein , nuclear protein , cell nucleus , nuclear export signal , microbiology and biotechnology , rna binding protein , biology , nuclear transport , estrogen receptor , chemistry , rna , biochemistry , nucleus , transcription factor , gene , genetics , cancer , breast cancer
Three proteins of a goat uterine small nuclear ribonucleoprotein (snRNP) fraction, which bind to nuclear estrogen receptor‐II (nER‐II) have been isolated and purified. These are the p32, p55, and p60 of which p32 is the major nER‐II binding protein. Indirect evidence reveals that p32 binds to the nuclear export signal (NES) on the nER‐II. nER‐II is a snRNA binding protein while p32 does not bind to the RNA. nER‐II along with p32 and p55 form an effective Mg ++ ATPase complex, the activation of which appears to be the immediate reason behind the RNP exit from the nuclei following estradiol exposure. The three nER‐II binding proteins bind to the nuclear pore complex; nER‐II does not possess this property. J. Cell. Biochem. 84: 227–236, 2002. © 2001 Wiley‐Liss, Inc.