CRM1 mediates nuclear export of nonstructural protein 2 from parvovirus minute virus of mice

被引：19

作者：

Ohshima, T

Nakajima, T

Oishi, T

Imamoto, N

Yoneda, Y

Fukamizu, A

Yagami, K ^{[1
]}

机构：

[1] Univ Tsukuba, Inst Basic Med, Tsukuba, Ibaraki 3058575, Japan

[2] Univ Tsukuba, Inst Appl Biochem, Tsukuba, Ibaraki, Japan

[3] Univ Tsukuba, Ctr Tsukuba Adv Res Alliance, Tsukuba, Ibaraki, Japan

[4] Osaka Univ, Sch Med, Dept Anat & Cell Biol, Osaka, Japan

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1999年 / 264卷 / 01期

基金：

日本学术振兴会;

关键词：

D O I：

10.1006/bbrc.1999.1478

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：

The nonstructural protein 2 (NS2) from parvovirus minute virus of mice (MVMp) is a 25-kDa polypeptide which localizes preferentially to the cytoplasm and associates with cellular proteins in cytoplasm. These lines of evidence suggest that NS2 is positively exported from the nucleus to cytoplasm and functions in cytoplasm. We report here that nuclear export of NS2 is inhibited by leptomycin B (LMB), a drug that specifically blocks nuclear export signal (NES)-chromosomal region maintenance 1 (CRM1) interactions. CRM1 binds specifically to the 81- to 106-amino-acid (aa) region of NS2, and the region of NS2 actually functions as a NES. Interestingly, this region appears to be distinct from a typical NES sequence, which consists of leucine-rich sequences. These results indicate that NS2 protein is continuously exported from the nucleus by a CRM1-dependent mechanism and suggest that CRM1 also exports to distinct type of NESs. (C) 1999 Academic Press.

引用

页码：144 / 150

页数：7

共 24 条

[1] Nonstructural proteins NS2 of minute virus of mice associate in vivo with 14-3-3 protein family members [J].