Role of MinD-membrane association in Min protein interactions.
Role of MinD-membrane association in Min protein interactions.
复制标题
MinD 膜关联在 Min 蛋白相互作用中的作用。
DOI:
10.1128/jb.188.8.2993-3001.2006
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发表时间:
2006
期刊:
影响因子:
--
通讯作者:
Rothfield,Lawrence
中科院分区:
文献类型:
--
作者:
Taghbalout,Aziz;Ma,Luyan;Rothfield,Lawrence
Division site placement inEscherichia coliinvolves interactions of the MinD protein with MinC and MinE and with other MinD molecules to form membrane-associated polymeric structures. In this work, as part of a study of these interactions, we established that heterologous membrane-associated proteins such as MinD can be targeted to the yeast nuclear membrane, dependent only on the presence of a membrane-binding domain and a nuclear targeting sequence. Targeting to the nuclear membrane was equally effective using the intrinsic MinD membrane-targeting domain or the completely unrelated membrane-targeting domain of cytochromeb5. The chimeric proteins differing in their membrane-targeting sequences were then used to establish the roles of membrane association and specificity of the membrane anchor in MinD interactions, using the yeast two-hybrid system. The chimeric proteins were also used to show that the membrane association of MinD and MinE inE. colicells had no specificity for the membrane anchor, whereas formation of MinDE polar zones and MinE rings required the presence of the native MinD membrane-targeting sequence.