大肠杆菌素A免疫蛋白与大肠杆菌内膜中大肠杆菌素A通道结构域的疏水螺旋发夹相互作用。
Colicin A immunity protein interacts with the hydrophobic helical hairpin of the colicin A channel domain in the Escherichia coli inner membrane.
作者信息
Nardi A, Corda Y, Baty D, Duché D
机构信息
Laboratoire d'Ingénierie des Systèmes Macromoléculaires, Institut de Biologie Structurale et Microbiologie, CNRS, Marseille, France.
出版信息
J Bacteriol. 2001 Nov;183(22):6721-5. doi: 10.1128/JB.183.22.6721-6725.2001.
Abstract
The colicin A pore-forming domain (pfColA) was fused to a bacterial signal peptide (sp-pfColA). This was inserted into the Escherichia coli inner membrane in functional form and could be coimmunoprecipitated with epitope-tagged immunity protein (EpCai). We constructed a series of fusion proteins in which various numbers of sp-pfColA alpha-helices were fused to alkaline phosphatase (AP). We showed that a fusion protein made up of the hydrophobic alpha-helices 8 and 9 of sp-pfColA fused to AP was specifically coimmunoprecipitated with EpCai produced in the same cells. This is the first biochemical evidence that Cai recognizes and interacts with the colicin A hydrophobic helical hairpin.
摘要
将大肠杆菌素A成孔结构域（pfColA）与细菌信号肽（sp-pfColA）融合。它以功能形式插入大肠杆菌内膜，并且可以与表位标签免疫蛋白（EpCai）进行共免疫沉淀。我们构建了一系列融合蛋白，其中将不同数量的sp-pfColAα螺旋与碱性磷酸酶（AP）融合。我们发现，由与AP融合的sp-pfColA的疏水α螺旋8和9组成的融合蛋白与同一细胞中产生的EpCai发生特异性共免疫沉淀。这是关于Cai识别并与大肠杆菌素A疏水螺旋发夹相互作用的首个生化证据。
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本文引用的文献
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Identification of specific residues in colicin E1 involved in immunity protein recognition.鉴定大肠杆菌素E1中参与免疫蛋白识别的特定残基。
J Bacteriol. 2001 Mar;183(6):2132-6. doi: 10.1128/JB.183.6.2132-2136.2001.
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Integration of the colicin A pore-forming domain into the cytoplasmic membrane of Escherichia coli.将大肠杆菌素A成孔结构域整合到大肠杆菌的细胞质膜中。
J Mol Biol. 1999 Feb 5;285(5):1965-75. doi: 10.1006/jmbi.1998.2423.
3
The tip of the hydrophobic hairpin of colicin U is dispensable for colicin U activity but is important for interaction with the immunity protein.大肠杆菌素U疏水发夹的末端对于大肠杆菌素U的活性并非必需，但对于与免疫蛋白的相互作用很重要。
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