CLONING OF A COMPLEMENTARY-DNA ENCODING AN 80 KILODALTON NUCLEAR CAP-BINDING PROTEIN

被引:42
作者
KATAOKA, N
OHNO, M
KANGAWA, K
TOKORO, Y
SHIMURA, Y
机构
[1] KYOTO UNIV, FAC SCI, DEPT BIOPHYS, KYOTO 606, JAPAN
[2] MIYAZAKI MED COLL, DEPT BIOCHEM, MIYAZAKI 88916, JAPAN
关键词
D O I
10.1093/nar/22.19.3861
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
It has been shown that the monomethylated cap structure plays important roles in nuclear events. The cap structure has been implicated in the enhancement of pre-mRNA splicing. More recently, this structure has also been suggested to facilitate RNA transport from the nucleus to the cytoplasm. We have previously identified and purified an 80kD Nuclear Cap Binding Protein (NCBP) from a HeLa cell nuclear extract, which could possibly mediate these nuclear activities. In this report, we describe cloning of complementary DNA (cDNA) encoding NCBP. The partial protein sequences of NCBP were determined, and the full-length cDNA of NCBP was isolated from HeLa cDNA libraries. This cDNA encoded an open reading frame of 790 amino acids with a calculated molecular mass of 91,734 daltons, which contained most of the determined protein sequences. However, the protein sequence had no significant homology to any known proteins. Transfection experiments demonstrated that the epitope-tagged NCBP, transiently expressed in HeLa cells, was localized exclusively in the nucleoplasm. Similar experiments using a truncated NCBP cDNA indicated that this nuclear localization activity is conferred by the N-terminal 70 amino-acid region.
引用
收藏
页码:3861 / 3865
页数:5
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