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Biochem Biophys Res Commun. 1999 Oct 14;264(1):144-50.

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

Author information

1
Institute of Basic Medicine, University of Tsukuba, Ibaraki, Japan.

Abstract

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.

PMID:
10527855
DOI:
10.1006/bbrc.1999.1478
[Indexed for MEDLINE]

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