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
复制标题
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
作者:
P. Glaser;D. Ladant;O. Sezer;F. Pichot;A. Ullmann;A. Danchin
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.
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
影响因子:
2.9
作者:
Shattuck,RL;Oldenburg,DJ;Storm,DR
通讯作者:
Storm,DR