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J. Biol. Chem., Vol. 279, Issue 36, 37751-37762, September 3, 2004

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The Bipartite Nuclear Localization Sequence of Rpn2 Is Required for Nuclear Import of Proteasomal Base Complexes via Karyopherin and Proteasome Functions^*

Petra Wendler, Andrea Lehmann, Katharina Janek, Sabine Baumgart, and Cordula Enenkel¶

From the Institut für Biochemie CCM, Charité, Universitätsmedizin Berlin, Monbijoustrasse 2, D-10117 Berlin, Germany

26 S proteasomes fulfill final steps in the ubiquitin-dependent degradation pathway by recognizing and hydrolyzing ubiquitylated proteins. As the 26 S proteasome mainly localizes to the nucleus in yeast, we addressed the question how this 2-MDa multisubunit complex is imported into the nucleus. 26 S proteasomes consist of a 20 S proteolytically active core and 19 S regulatory particles, the latter composed of two subcomplexes, namely the base and lid complexes. We have shown that 20 S core particles are translocated into the nucleus as inactive precursor complexes via the classic karyopherin import pathway. Here, we provide evidence that nuclear import of base and lid complexes also depends on karyopherin . Potential classic nuclear localization sequences (NLSs) of base subunits were analyzed. Rpn2 and Rpt2, a non-ATPase subunit and an ATPase subunit of the base complex, harbor functional NLSs. The Rpt2 NLS deletion yielded wild type localization. However, the deletion of the Rpn2 NLS resulted in improper nuclear proteasome localization and impaired proteasome function. Our data support the model by which nuclear 26 S proteasomes are assembled from subcomplexes imported by karyopherin

Received for publication, March 31, 2004 , and in revised form, June 11, 2004.

^* This work was supported in part by the Deutsche Forschungsgemeinschaft (Grant EN 301/4-4 to C. E.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains Figs. S1 and S2.

Present address: School of Crystallography, Birkbeck College, Malet St., London WC1E 7HX, United Kingdom.

Supported by a project to Peter-Michael Kloetzel from the Bundesministerium für Bildung und Forschung.

^¶ To whom correspondence should be addressed. Tel.: 49-30-450-528-158; Fax: 49-30-450-528-916; E-mail: cordula.enenkel{at}charite.de.

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