The nuclear import of RNA helicase A is mediated by importin-α3

被引:41
|
作者
Oishi, T
Fujita, H
Nakazawa, M
Fujii, R
Imamoto, N
Yoneda, Y
Fukamizu, A
Nakajima, T
机构
[1] St Marianna Univ, Sch Med, Inst Med Sci, Dept Genome Sci, Kawasaki, Kanagawa 2168512, Japan
[2] Univ Tsukuba, Grad Sch Life & Environm Sci, Ctr Tsukuba Adv Res Alliance, Tsukuba, Ibaraki 3058572, Japan
[3] RIKEN, Discovery Res Inst, Cellular Dynam Lab, Wako, Saitama 3510198, Japan
[4] Osaka Univ, Grad Sch Frontier Biosci, Dept Frontier Biosci, Suita, Osaka 5650871, Japan
基金
日本学术振兴会;
关键词
RNA helicase A; nuclear localization signal; importin;
D O I
10.1016/j.bbrc.2005.11.161
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
RNA helicase A (RHA), an ATPase/helicase, regulates the gene expression at various steps including transcriptional activation and RNA processing. RHA is known to shuttle between the nucleus and cytoplasm. We identified the nuclear localization signal (NLS) of RHA and analyzed the nuclear import mechanisms. The NLS of RHA (RHA-NLS) consisting of 19 amino acid residues is highly conserved through species and does not have the consensus classical NLS. In vitro nuclear import assays revealed that the nuclear import of RHA was Ran-dependent and mediated with the classical importin-alpha/beta-dependent pathway. The binding assay indicated that the basic residues in RHA-NLS were used for interaction with importin-alpha. Furthermore, the nuclear import of RHA-NLS was supported by importin-alpha 1 and preferentially importin-alpha 3. Our results indicate that the nuclear import of RHA is mediated by the importin-alpha 3/importin-beta-dependent pathway and suggest that the specificity for importin may regulate the functions of cargo proteins. (c) 2005 Elsevier Inc. All rights reserved.
引用
收藏
页码:125 / 133
页数:9
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