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Updated: May 29, 2025

Functional Characterization of RING-Type E3 Ubiquitin Ligases In Vitro and In Planta

Functional Characterization of RING-Type E3 Ubiquitin Ligases In Vitro and In Planta

Published on: December 5, 2019

环二度化驱动SINA/SIAH E3泛基因酶的更高阶组织

Franck Coste¹, Aanchal Mishra^1,2, Catherine Chapuis³

¹Centre de Biophysique Moléculaire (CBM), UPR 4301, CNRS, Orléans, France.

The FEBS journal

|February 5, 2025

概括

SIAH1 E3酶RING域二元化增强了它的活性,并形成了更高阶结构. 这种多元化对于SIAH1至关重要.

科学领域:

生物化学生物化学
分子生物学分子生物学
结构生物学结构生物学

背景情况:

环型E3泛素连接酶对于泛化至关重要.
SIAH1使用一种催化RING域和一种基质结合域 (SBD).
之前的研究表明,SINA/SIAH链酶中SBD介导的同质化.

研究的目的:

为了确定SIAH1 RING域的晶体结构.
调查RING域二分化在SIAH1 E3酶活性中的作用.
为了阐明SINA/SIAH E3结合酶的高级组合.

主要方法:

人类SIAH1 RING域的X射线晶体学.
静态光散射以验证溶液中的二分化.
使用光标记蛋白质进行细胞局部化研究.
同局部化测试与聚合的synphilin-1A.

主要成果:

晶体结构揭示了人类SIAH1.1的潜在RING二元体.
在溶液中证实了RING二分化,并在体外和细胞内增强SIAH1 E3酶活性.
SIAH1,SIAH2和SINA形成了细胞质群,在禁用RING二分化时被破坏.
野生型SIAH1,但不是其二分化突变,与聚合的synphilin-1A.同位素化.

结论:

环域二分化是SIAH1 E3结合酶功能的一个关键特征.
交替的RING:RING和SBD:SBD相互作用可能会将SINA/SIAH蛋白组织成更高阶的同质多元体.
SIAH1的多元化可能有助于其对聚合蛋白的基质偏好.

关键词:

E3 无处不在的合酶在RING域名域名中.一个SIAH1公司.蛋白质的多重化.无处不在的无处不在关系

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In Vitro Analysis of E3 Ubiquitin Ligase Function

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Published on: May 14, 2021

In Vitro Ubiquitination and Deubiquitination Assays of Nucleosomal Histones

In Vitro Ubiquitination and Deubiquitination Assays of Nucleosomal Histones

Published on: July 25, 2019

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