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© The Rockefeller University Press, 0021-9525/1998//1415 $5.00
The Journal of Cell Biology, Volume 141, Number 6, , 1998 1415-1422

Articles

A Giant Ubiquitin-conjugating Enzyme Related to IAP Apoptosis Inhibitors



Hans-Peter Hauser*, Michael Bardroff{ddagger}, George Pyrowolakis{ddagger}, and Stefan Jentsch{ddagger}

* Friedrich-Miescher-Laboratorium der Max-Planck-Gesellschaft, 72076 Tübingen, Germany; and {ddagger} ZMBH, Zentrum für Molekulare Biologie, Universität Heidelberg, D-69120 Heidelberg, Germany

Ubiquitin-conjugating enzymes (UBC) catalyze the covalent attachment of ubiquitin to target proteins and are distinguished by the presence of a UBC domain required for catalysis. Previously identified members of this enzyme family are small proteins and function primarily in selective proteolysis pathways. Here we describe BRUCE (BIR repeat containing ubiquitin-conjugating enzyme), a giant (528-kD) ubiquitin-conjugating enzyme from mice. BRUCE is membrane associated and localizes to the Golgi compartment and the vesicular system. Remarkably, in addition to being an active ubiquitin-conjugating enzyme, BRUCE bears a baculovirus inhibitor of apoptosis repeat (BIR) motif, which to this date has been exclusively found in apoptosis inhibitors of the IAP-related protein family. The BIR motifs of IAP proteins are indispensable for their anti–cell death activity and are thought to function through protein–protein interaction. This suggests that BRUCE may combine properties of IAP-like proteins and ubiquitin-conjugating enzymes and indicates that the family of IAP-like proteins is structurally and functionally more diverse than previously expected.

Abbreviations used in this paper: BIR, baculovirus inhibitor of apoptosis repeat; BRUCE, BIR repeat containing ubiquitin-conjugating enzyme; E1, ubiquitin-activating enzyme; IAP, inhibitor of apoptosis protein; NAIP, neuronal apoptosis inhibitor protein; ORF, open reading frame; UBC, ubiquitin-conjugating enzyme.

The work by H.-P. Hauser was done in the former laboratory of S. Jentsch in Tübingen. We thank T. Hoppe for important contributions to this study; M. Scheffner, G. Banting, R. Brandt, B. Dobberstein, and A. Clement for providing materials; M. Scheffner for help and advice for thioester experiments; F. Weinreich for help with DNA sequencing; E. Löser and P. Hubbe for technical assistance; and H. Ulrich for comments on the manuscript.

H.-P. Hauser and M. Bardroff contributed equally to this work.

Address all correspondence to Dr. Stefan Jentsch, ZMBH, Zentrum für Molekulare Biologie, Universität Heidelberg, Im Neuenheimer Feld 282, D-69120 Heidelberg, Germany. Tel.: +49 6221 548716. Fax: 49 6221 545891. E-mail: jentsch{at}zmbh.uni-heidelberg.de

The present address of Hans-Peter Hauser is Dade Behring, Inc., M 106, P.O. Box 1149, 35001 Marburg, Germany.

The present address of Michael Bardroff is MorphoSys GmbH, Am Klopferspitz 19, 82152 Martinsried/Munich, Germany.


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