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Activation of a primed RING E3-E2-ubiquitin complex by non-covalent ubiquitin.

Abstract：

:RING ubiquitin ligases (E3) recruit ubiquitin-conjugate enzymes (E2) charged with ubiquitin (Ub) to catalyze ubiquitination. Non-covalent Ub binding to the backside of certain E2s promotes processive polyUb formation, but the mechanism remains elusive. Here, we show that backside bound Ub (Ub(B)) enhances both RING-independent and RING-dependent UbcH5B-catalyzed donor Ub (Ub(D)) transfer, but with a more prominent effect in RING-dependent transfer. Ub(B) enhances RING E3s' affinities for UbcH5B-Ub, and RING E3-UbcH5B-Ub complex improves Ub(B)'s affinity for UbcH5B. A comparison of the crystal structures of a RING E3, RNF38, bound to UbcH5B-Ub in the absence and presence of Ub(B), together with molecular dynamics simulation and biochemical analyses, suggests Ub(B) restricts the flexibility of UbcH5B's α1 and α1β1 loop. Ub(B) supports E3 function by stabilizing the RING E3-UbcH5B-Ub complex, thereby improving the catalytic efficiency of Ub transfer. Thus, Ub(B) serves as an allosteric activator of RING E3-mediated Ub transfer.

journal_name

Mol Cell

journal_title

Molecular cell

authors

Buetow L,Gabrielsen M,Anthony NG,Dou H,Patel A,Aitkenhead H,Sibbet GJ,Smith BO,Huang DT

doi

10.1016/j.molcel.2015.02.017

subject

Has Abstract

pub_date

2015-04-16 00:00:00

pages

297-310

issue

2

eissn

1097-2765

issn

1097-4164

pii

S1097-2765(15)00131-8

journal_volume

58

pub_type

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