Department of Physiology and Biophysics and Developmental and Cell Biology, University of California, Irvine, California 92697, USA.
Mol Cell Proteomics. 2011 Jan;10(1):M110.002212. doi: 10.1074/mcp.M110.002212. Epub 2010 Aug 24.
Knowledge of elaborate structures of protein complexes is fundamental for understanding their functions and regulations. Although cross-linking coupled with mass spectrometry (MS) has been presented as a feasible strategy for structural elucidation of large multisubunit protein complexes, this method has proven challenging because of technical difficulties in unambiguous identification of cross-linked peptides and determination of cross-linked sites by MS analysis. In this work, we developed a novel cross-linking strategy using a newly designed MS-cleavable cross-linker, disuccinimidyl sulfoxide (DSSO). DSSO contains two symmetric collision-induced dissociation (CID)-cleavable sites that allow effective identification of DSSO-cross-linked peptides based on their distinct fragmentation patterns unique to cross-linking types (i.e. interlink, intralink, and dead end). The CID-induced separation of interlinked peptides in MS/MS permits MS(3) analysis of single peptide chain fragment ions with defined modifications (due to DSSO remnants) for easy interpretation and unambiguous identification using existing database searching tools. Integration of data analyses from three generated data sets (MS, MS/MS, and MS(3)) allows high confidence identification of DSSO cross-linked peptides. The efficacy of the newly developed DSSO-based cross-linking strategy was demonstrated using model peptides and proteins. In addition, this method was successfully used for structural characterization of the yeast 20 S proteasome complex. In total, 13 non-redundant interlinked peptides of the 20 S proteasome were identified, representing the first application of an MS-cleavable cross-linker for the characterization of a multisubunit protein complex. Given its effectiveness and simplicity, this cross-linking strategy can find a broad range of applications in elucidating the structural topology of proteins and protein complexes.
蛋白质复合物精细结构的知识对于理解其功能和调控机制至关重要。尽管交联结合质谱(MS)已被提出作为解析大的多亚基蛋白质复合物结构的可行策略,但由于通过 MS 分析明确鉴定交联肽和确定交联位点的技术困难,该方法具有挑战性。在这项工作中,我们开发了一种使用新设计的 MS 可切割交联剂二琥珀酰亚胺基磺酸盐(DSSO)的新型交联策略。DSSO 包含两个对称的碰撞诱导解离(CID)可切割位点,允许根据交联类型(即交联、内连和死端)特有的独特碎裂模式有效鉴定 DSSO 交联肽。在 MS/MS 中,CID 诱导的交联肽分离允许对具有定义修饰(由于 DSSO 残留物)的单个肽链片段离子进行 MS(3)分析,以便使用现有的数据库搜索工具进行简单解释和明确鉴定。来自三个生成数据集(MS、MS/MS 和 MS(3))的数据分析的整合允许高度置信地鉴定 DSSO 交联肽。使用模型肽和蛋白质证明了新开发的基于 DSSO 的交联策略的功效。此外,该方法成功用于酵母 20S 蛋白酶体复合物的结构表征。总共鉴定了 20S 蛋白酶体的 13 个非冗余交联肽,这代表了首次使用 MS 可切割交联剂对多亚基蛋白质复合物进行表征。鉴于其有效性和简单性,这种交联策略可以在阐明蛋白质和蛋白质复合物的结构拓扑方面找到广泛的应用。