Role of E2-RING Interactions in Governing RNF4-Mediated Substrate Ubiquitination
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- 作者：Anthony DiBello1 ; Ajit B. Datta ; Xiangbin Zhang ; Cynthia Wolberger ; cwolberg@jhmi.edu" class="auth_mail" title="E-mail the corresponding author
- 关键词：Ub ; ubiquitin ; E1 ; Ub-activating enzyme ; E2 ; Ub-conjugating enzyme ; E3 ; Ub ligase ; RING ; really interesting new gene ; GST ; glutathione S-transferase ; RNF4 ; RING finger protein 4 ; UbMe ; methylated Ub ; RAD6Bs5B ; RAD6B surface conversion mutants of UBCH5B ; SE ; sedimentation equilibrium ; SE-AUC ; sedimentation equilibrium analytical ultracentrifugation ; UbFL ; fluorescein-labeled ubiquitin ; TRX ; thioredoxin ; TEV ; tobacco etch virus ; BME ; β-mercaptoethanol ; IMAC ; immobilized metal affinity chromatograp
- 刊名：Journal of Molecular Biology
- 出版年：2016
- 出版时间：20 November 2016
- 年：2016
- 卷：428
- 期：23
- 页码：4639-4650
- 全文大小：1108 K
文摘
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Ubiquitination activity on polySUMO substrates by RNF4 is E2-dependent.
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Reengineered RAD6B RING-binding surface transforms substrate ubiquitination activity.
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Increased UBCH5B-like RING-binding surface drives polyubiquitination.
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Increased UBCH5B-like RING-binding surface confers greater E2–RNF4 affinity.
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E2–E3 affinity governs multiplicity of RNF4-mediated polyubiquitination of substrates.