Large-scale identification of protein-protein interaction of Escherichia coli K-12
Large-scale identification of protein-protein interaction of Escherichia coli K-12
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DOI：
10.1101/gr.4527806
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发表时间：
2006-05-01
期刊：
影响因子：
7
通讯作者：
Mori, H
中科院分区：
文献类型：
--
作者：
Arifuzzaman, M;Maeda, M;Mori, H
蛋白质之间的相互作用在蛋白质的功能和细胞的结构组织中起着关键作用。对这些相互作用的透彻描述应该有助于阐明细胞活动、靶向药物设计和全细胞工程。使用组氨酸标记的大肠杆菌ORF克隆文库进行了大规模的综合下拉分析。在测试的4339个诱饵蛋白中，找到了2667个蛋白，其中包括779个功能未知的蛋白。用基质辅助激光解吸电离飞行时间质谱仪(MALDI-TOF MS)鉴定了Ni2+-NTA色谱柱上与六组氨酸标记的诱饵共纯化的蛋白质。通过生物信息学和实验对这些相互作用的网络进行扩展分析，应该会为大肠杆菌系统生物学提供新的见解和新的策略。
Protein-protein interactions play key roles in protein function and the structural organization of a cell. A thorough description of these interactions should facilitate elucidation of cellular activities, targeted-drug design, and whole cell engineering. A large-scale comprehensive pull-down assay was performed using a His-tagged Escherichia coli ORF clone library. Of 4339 bait proteins tested, partners were found for 2667, including 779 of unknown function. Proteins copurifying with hexahistidine-tagged baits on a Ni2+-NTA column were identified by MALDI-TOF MS (matrix-assisted laser desorption ionization time of flight mass spectrometry). An extended analysis of these interacting networks by bioinformatics and experimentation should provide new insights and novel strategies for E. coli systems biology.