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. 2015 Apr 2;467(Pt 2):345–352. doi: 10.1042/BJ20141502

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© 2015 This is an Open Access article distributed under the terms of the Creative Commons Attribution Licence (CC-BY)(http://creativecommons.org/licenses/by/3.0/) which permits unrestricted use, distribution and reproduction in any medium, provided the original work is properly cited.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution and reproduction in any medium, provided the original work is properly cited.

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(A) Ubiquitylation assays of AREL1 in the presence of UBE1, UBE2D1 and wild-type Ub or Ub mutants that have only one or no lysine residue. (B) Large-scale assembly of polyUb chains by AREL1 in the presence of UBE1, UBE2D1 and Ub. The addition of DUBs, Cezanne EK and OTUB1, releases free polyUb chains. (C) Ubiquitylation assays of AREL1 in the presence of UBE1, UBE2D1 and wild-type Ub or lysine-to-arginine Ub mutants. DUBs, Cezanne EK and OTUB1, were added after 3 h of reaction. (D) Auto-ubiquitylation assays of AREL1 as in (A) with wild-type Ub. DUBs, Cezanne EK, OTUB1 and TRABID, were added after 3 h reaction as indicated. (E) Purification of Lys³³-linked chains of defined lengths by cation-exchange chromatography. (F) The Lys³³-linked diUb and triUb purified in (D) were visualized in silver-stained SDS gel.