RING Dimerization Links Higher-Order Assembly of TRIM5α to Synthesis of K63-Linked Polyubiquitin.
作者： Zinaida Yudina , Amanda Roa , Rory Johnson , Nikolaos Biris , Daniel A. de Souza Aranha Vieira
DOI: 10.1016/J.CELREP.2015.06.072
关键词:
摘要: Summary Members of the tripartite motif (TRIM) protein family of RING E3 ubiquitin (Ub) ligases promote innate immune responses by catalyzing synthesis polyubiquitin chains linked through lysine 63 (K63). Here, we investigate mechanism which TRIM5α retroviral restriction factor activates Ubc13, K63-linkage-specific E2. Structural, biochemical, and functional characterization TRIM5α:Ubc13-Ub interactions reveals that activation Ubc13-Ub conjugate requires dimerization RING domain. Our data explain how higher-order oligomerization TRIM5α, is promoted interaction with capsid, enhances E3 Ub ligase activity contributes to its antiretroviral function. This mechanism, in transient depends on TRIM ligand, likely be conserved many members may have evolved facilitate recognition repetitive epitope patterns associated infection.
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