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J. Biol. Chem., Vol. 281, Issue 35, 25502-25508, September 1, 2006

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The PUB Domain Functions as a p97 Binding Module in Human Peptide N-Glycanase^*

Mark D. Allen, Alexander Buchberger¹, and Mark Bycroft²

From the Centre for Protein Engineering, Medical Research Council, Hills Road, Cambridge CB2 2QH, United Kingdom and the Max Planck Institute of Biochemistry, Department of Molecular Cell Biology, Am Klopferspitz 18, 82152 Martinsried, Germany

The AAA ATPase p97 is a ubiquitin-selective molecular machine involved in multiple cellular processes, including protein degradation through the ubiquitin-proteasome system and homotypic membrane fusion. Specific p97 functions are mediated by a variety of cofactors, among them peptide N-glycanase, an enzyme that removes glycans from misfolded glycoproteins. Here we report the three-dimensional structure of the aminoterminal PUB domain of human peptide N-glycanase. We demonstrate that the PUB domain is a novel p97 binding module interacting with the D1 and/or D2 ATPase domains of p97 and identify an evolutionary conserved surface patch required for p97 binding. Furthermore, we show that the PUB and UBX domains do not bind to p97 in a mutually exclusive manner. Our results suggest that PUB domain-containing proteins constitute a widespread family of diverse p97 cofactors.

Received for publication, February 7, 2006 , and in revised form, June 27, 2006.

^* This work was supported by Emmy Noether Grant Bu 951/1-1 to /1-4 of the Deutsche Forschungsgemeinschaft (to A. B.). 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.

¹ To whom correspondence may be addressed. Tel.: 49-89-85783050; Fax: 49-89-85783055; E-mail: buchberg{at}biochem.mpg.de. ² To whom correspondence may be addressed. Tel.: 44-1223-402129; Fax: 44-1223-402140; E-mail: mb10031{at}cus.cam.ac.uk.

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