Fig. 4: The mechanism of RING-anchored ubiquitination in cis. | Nature Communications

Fig. 4: The mechanism of RING-anchored ubiquitination in cis.

From: RING domains act as both substrate and enzyme in a catalytic arrangement to drive self-anchored ubiquitination

Fig. 4

a For ubiquitination in cis, the RING-anchored (blue) ubiquitin chain (red) must be sufficiently long to reach the active site on Ube2N~Ub/Ube2V2 (Ube2N in green, Ub in orange, and Ube2V2 in teal). The chain can go around two different routes, one shown here and the other in Supplementary Fig. 10. The ubiquitin chain was modeled using the Ub-R:Ube2N~Ub:Ube2V2 structure and a K63-linked Ub2 structure (2JF5 (ref. 34)) using PyMol. b Substrate (Fc)-induced self-ubiquitination assay of 100 nM Ubn-TRIM21 constructs. Reactions were incubated for 5 min at 37 °C. Western blots are representative of n = 3 independently performed experiments. Uncropped blots are provided in Source data. Ub ubiquitin, R RING, PS PRYSPRY, kDa kilo Dalton.

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