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Interaction network containing conserved and essential protein complexes in Escherichia coli

机译：包含保守和必需蛋白质复合物的大肠杆菌相互作用网络

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摘要

Proteins often function as components of multi-subunit complexes. Despite its long history as a model organism(1), no large-scale analysis of protein complexes in Escherichia coli has yet been reported. To this end, we have targeted DNA cassettes into the E. coli chromosome to create carboxy-terminal, affinity-tagged alleles of 1,000 open reading frames (similar to23% of the genome). A total of 857 proteins, including 198 of the most highly conserved, soluble non-ribosomal proteins essential in at least one bacterial species, were tagged successfully, whereas 648 could be purified to homogeneity and their interacting protein partners identified by mass spectrometry. An interaction network of protein complexes involved in diverse biological processes was uncovered and validated by sequential rounds of tagging and purification. This network includes many new interactions as well as interactions predicted based solely on genomic inference or limited phenotypic data(2). This study provides insight into the function of previously uncharacterized bacterial proteins and the overall topology of a microbial interaction network, the core components of which are broadly conserved across Prokaryota.
机译：蛋白质通常充当多亚基复合物的成分。尽管它作为模型有机体已有悠久的历史（1），但尚未报道对大肠杆菌中蛋白质复合物进行大规模分析的报道。为此，我们将DNA盒靶向大肠杆菌染色体，以创建具有1,000个开放阅读框的羧基末端，亲和标签的等位基因（约占基因组的23％）。总共成功标记了857种蛋白质，其中包括至少一种细菌中必不可少的198种最高度保守的可溶性非核糖体蛋白质，而可以纯化648种蛋白质，使其具有同质性，并且可以通过质谱鉴定其相互作用的蛋白质伴侣。揭示了参与多种生物过程的蛋白质复合物的相互作用网络，并通过顺序的标记和纯化步骤进行了验证。该网络包括许多新的相互作用以及仅基于基因组推论或有限的表型数据预测的相互作用（2）。这项研究深入了解了以前未鉴定的细菌蛋白的功能以及微生物相互作用网络的整体拓扑，而微生物相互作用网络的核心组成部分在原核生物中被广泛保存。

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