## Abstract Exposure of goat uterine nuclei to estradiol in vitro results in an immediate exit of ribonucleoproteins (RNP) from the nuclei to the medium. This RNP exit appears to be mediated by an estrogen receptor localized in small nuclear ribonucleoproteins containing U1 and U2 snRNA. Available
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
✍ Scribed by Thomas Sebastian; Raghava Varman Thampan
- Publisher
- John Wiley and Sons
- Year
- 2002
- Tongue
- English
- Weight
- 212 KB
- Volume
- 84
- Category
- Article
- ISSN
- 0730-2312
- DOI
- 10.1002/jcb.1280
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✦ Synopsis
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. J. Cell. Biochem. 84: 227–236, 2002. © 2001 Wiley‐Liss, Inc.
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