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  The importin-beta binding domain of snurportin1 is responsible for the Ran- and energy-independent nuclear import of spliceosomal U snRNPs in vitro

Huber, J., Dickmanns, A., & Luehrmann, R. (2002). The importin-beta binding domain of snurportin1 is responsible for the Ran- and energy-independent nuclear import of spliceosomal U snRNPs in vitro. Journal of Cell Biology, 156(3), 467-479. Retrieved from http://jcb.rupress.org/content/156/3/467.full.pdf+html.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0010-942B-0 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-9CB7-B
Genre: Journal Article

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Huber, J., Author
Dickmanns, A., Author
Luehrmann, R.1, Author              
Affiliations:
1Department of Cellular Biochemistry, MPI for biophysical chemistry, Max Planck Society, ou_578576              

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Free keywords: spliceosomal U snRNPs; IBB domain; snurportin 1; nucleocytoplasmic transport; energy and Ran requirements
 Abstract: The nuclear localization signal (NLS) of spliceosomal U snRNPs is composed of the U snRNA's 2,2,7-trimethyl-guanosine (m(3)G)- cap and the Sm core domain. The m(3)G-cap is specifically bound by snurportin1, which contains an NH2-terminal importin-beta binding (IIB) domain and a COOH-terminal m(3)G-cap-binding region that bears no structural similarity to known import adaptors like importin-alpha (impalpha). Here, we show that recombinant snurportin1 and importin-beta (impbeta) are not only necessary, but also sufficient for U1 snRNP transport to the nuclei of digitonin-permeabilized HeLa cells. In contrast to impalpha-dependent import, single rounds of U1 snRNP import, mediated by the nuclear import receptor complex snurportin1- impbeta, did not require Ran and energy. The same Ran and energy-independent import was even observed for U5 snRNP, which has a molecular weight of more than one million. Interestingly, in the presence of impbeta and a snurportin1 mutant containing an impa IIB domain (IBBimpalpha), nuclear U1 snRNP import was Ran dependent. Furthermore, beta-galactosidase (betaGal) containing a snurportin1 IIB domain, but not IIBimpalpha- betaGal, was imported into the nucleus in a Ran-independent manner. Our results suggest that the nature of the IBB domain modulates the strength and/or site of interaction of impbeta with nucleoporins of the nuclear pore complex, and thus whether or not Ran is required to dissociate these interactions.

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Language(s): eng - English
 Dates: 2002-02-04
 Publication Status: Published in print
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 Rev. Method: Peer
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Title: Journal of Cell Biology
Source Genre: Journal
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Pages: - Volume / Issue: 156 (3) Sequence Number: - Start / End Page: 467 - 479 Identifier: -