The calmodulin‐sensitive adenylate cyclase of Bordetella pertussis: cloning and expression in Escherichia col

The calmodulin‐sensitive adenylate cyclase of Bordetella pertussis: cloning and expression in Escherichia col
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百日咳博德特氏菌钙调素敏感腺苷酸环化酶:在大肠杆菌中的克隆和表达

DOI:
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发表时间:
1988
影响因子:
3.6
通讯作者:
A. Danchin
A. Danchin
中科院分区:
生物学2区
文献类型:
--
作者:
P. Glaser;D. Ladant;O. Sezer;F. Pichot;A. Ullmann;A. Danchin

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原核生物百日咳杆菌的腺苷酸环化酶毒素受真核生物调节蛋白钙调蛋白的刺激。一般策略,使用腺苷酸-环化酶-钙调蛋白相互作用作为工具,允许在不存在任何B的情况下在大肠杆菌中克隆和表达毒素。百日咳反式激活因子。我们表明,蛋白质是合成的一个大的前体形式组成的1706个氨基酸。钙调素刺激的催化活性存在于腺苷酸环化酶的氨基末端450个氨基酸中。在E.在Western印迹中,针对纯化的B的抗体识别大肠杆菌。百日咳腺苷酸环化酶,并且其活性被这些抗体抑制。
The adenylate cyclase toxin of the prokaryote Bordetella pertussis is stimulated by the eukaryotic regulatory protein, calmodulin. A general strategy, using the adenylate‐cyclase‐calmodulin interaction as a tool, has permitted cloning and expression of the toxin in Escherichia coli in the absence of any B. pertussis trans‐activating factor. We show that the protein is synthesized in a large precursor form composed of 1706 amino acids. The calmodulin‐stimulated catalytic activity resides in the amino‐terminal 450 amino acids of the adenylate cyclase. The enzyme expressed in E. coli is recognized in Western blots by antibodies directed against purified B. pertussis adenylate cyclase, and its activity is inhibited by these antibodies.
设计用于位点特异性诱变的钙调蛋白基因的化学合成和表达。
DOI: 10.1021/bi00340a020
发表时间: 1985
期刊: Biochemistry
影响因子: 2.9
作者:
Roberts,DM;Crea,R;Malecha,M;Alvarado-Urbina,G;Chiarello,RH;Watterson,DM
通讯作者: Watterson,DM
百日咳博德特氏菌中钙调蛋白敏感的腺苷酸环化酶的纯化和表征。
DOI: 10.1021/bi00344a006
发表时间: 1985
期刊: Biochemistry
影响因子: 2.9
作者:
Shattuck,RL;Oldenburg,DJ;Storm,DR
通讯作者: Storm,DR