The distinction between pleiotrotic and moonlighting roles of proteins is challenging; however, this distinction may be clearer when it comes to multiprotein complexes. Two examples are the proteasome lid and the COP9 signalosome (CSN), which are twin enzymes with 1:1 paralogy between subunits. In each complex, one out of eight subunits harbours a JAMM/MPN+ metalloprotease motif. This motif contributes the canonical activity of each complex: hydrolysis of covalently attached ubiquitin by Rpn11 in the proteasome lid and hydrolysis of ubiquitin-related 1 (Rub1/Nedd8) from Cullins by Csn5 in the CSN. In both complexes, executing this activity suggests pleiotropic effects and requires an assembled full complex. However, beyond canonical functions, both Rpn11 and Csn5 are involved in additional unique, complex-independent functions, herein referred to as moonlighting activities.
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December 2014
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Conference Article|
November 17 2014
Moonlighting and pleiotropy within two regulators of the degradation machinery: the proteasome lid and the CSN
Elah Pick;
Elah Pick
1
*Department of Biology and Environment, Faculty of Natural Sciences, University of Haifa at Oranim, Tivon 3003500, Israel
†Department of Human Biology, Faculty of Natural Sciences, University of Haifa, Haifa 3498838, Israel
1To whom correspondence should be addressed (emailelahpic@research.haifa.ac.il).
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Laylan Bramasole
Laylan Bramasole
†Department of Human Biology, Faculty of Natural Sciences, University of Haifa, Haifa 3498838, Israel
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Publisher: Portland Press Ltd
Received:
August 26 2014
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© The Authors Journal compilation © 2014 Biochemical Society
2014
Biochem Soc Trans (2014) 42 (6): 1786–1791.
Article history
Received:
August 26 2014
Citation
Elah Pick, Laylan Bramasole; Moonlighting and pleiotropy within two regulators of the degradation machinery: the proteasome lid and the CSN. Biochem Soc Trans 1 December 2014; 42 (6): 1786–1791. doi: https://doi.org/10.1042/BST20140227
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