| Literature DB >> 11787052 |
Thomas Sebastian1, Raghava Varman Thampan.
Abstract
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. Copyright 2001 Wiley-Liss, Inc.Entities:
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Year: 2002 PMID: 11787052 DOI: 10.1002/jcb.1280
Source DB: PubMed Journal: J Cell Biochem ISSN: 0730-2312 Impact factor: 4.429