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K29-Selective Ubiquitin Binding Domain Reveals Structural Basis of Specificity and Heterotypic Nature of K29 Polyubiquitin

DOI: 10.1016/j.molcel.2015.01.041 DOI Help
PMID: 25752573 PMID Help

Authors: Yosua adi Kristariyanto (University of Dundee) , Syed arif Abdul rehman (University of Dundee) , David g Campbell (University of Dundee) , Nicholas a Morrice (University of Dundee) , Clare Johnson (University of Dundee) , Rachel Toth (University of Dundee) , Yogesh Kulathu (University of Dundee)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Molecular Cell , VOL 58 (1) , PAGES 1-12

State: Published (Approved)
Published: April 2015
Diamond Proposal Number(s): 8268

Open Access Open Access

Abstract: Polyubiquitin chains regulate diverse cellular pro- cesses through the ability of ubiquitin to form chains of eight different linkage types. Although detected in yeast and mammals, little is known about K29-linked polyubiquitin. Here we report the generation of K29 chains in vitro using a ubiquitin-chain editing com- plex consisting of the HECT E3 ligase UBE3C and the deubiquitinase vOTU. We determined the crystal structure of K29-linked diubiquitin, which adopts an extended conformation with the hydrophobic patches on both ubiquitin moieties exposed and available for binding. Indeed, the crystal structure of the NZF1 domain of TRABID in complex with K29 chains reveals a binding mode that involves the hydrophobic patch on only one of the ubiquitin moi- eties and exploits the flexibility of K29 chains to achieve linkage selective binding. Further, we estab- lish methods to study K29-linked polyubiquitin and find that K29 linkages exist in cells within mixed or branched chains containing other linkages.

Subject Areas: Biology and Bio-materials


Instruments: I24-Microfocus Macromolecular Crystallography

Other Facilities: ESRF

Added On: 21/03/2015 06:27

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