Purification and identification of endogenous polySUMO conjugates
Purification and identification of endogenous polySUMO conjugates
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DOI：
10.1038/embor.2010.206
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发表时间：
2011-02-01
期刊：
影响因子：
7.7
通讯作者：
Hay, Ronald T.
中科院分区：
文献类型：
--
作者：
Bruderer, Roland;Tatham, Michael H.;Hay, Ronald T.
小的泛素样修饰物(SUMO)可以自我修饰，形成多聚链，参与细胞减数分裂、基因组维持和胁迫反应等过程。由于缺乏与相扑链链相连的蛋白质的纯化方案，对聚合链的生物学作用的研究一直受到阻碍。在本文中，我们描述了一种快速亲和纯化方法，用于分离内源性PolySUMO修饰物种，产生适合于个体蛋白质研究和蛋白质组分析的高纯度物质。我们使用这种方法从培养的真核细胞中鉴定了300多个假定的PolySUMO结合物。
The small ubiquitin-like modifier (SUMO) can undergo self-modification to form polymeric chains that have been implicated in cellular processes such as meiosis, genome maintenance and stress response. Investigations into the biological role of polymeric chains have been hampered by the absence of a protocol for the purification of proteins linked to SUMO chains. In this paper, we describe a rapid affinity purification procedure for the isolation of endogenous polySUMO-modified species that generates highly purified material suitable for individual protein studies and proteomic analysis. We use this approach to identify more than 300 putative polySUMO conjugates from cultured eukaryotic cells.