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. Author manuscript; available in PMC: 2011 Feb 1.
Published in final edited form as: Nat Struct Mol Biol. 2010 Jul 11;17(8):939–947. doi: 10.1038/nsmb.1873

Figure 2.

Figure 2

Assembly of Lys11-linked diubiquitin

(a) Domain structure of UBE2S, and autoubiquitination reactions with UBE2S wild-type and catalytic mutants. (b) UBE2S autoubiquitination occurs in cis. Wild-type UBE2S was mixed with GST-tagged inactive UBE2SC95A, and after precipitation of the GST-tagged protein, ubiquitination in supernatant (left) and precipitate (right) is analyzed. (c) Removal of the Lys-rich tail of UBE2S decreases autoubiquitination while preserving Lys11 specificity. (d) Purification of Lys11-linked diubiquitin by cation exchange chromatography. The integrated peak area (mAU*ml) is indicated. A gel showing protein-containing fractions is shown as an inset.