Role of MinD-membrane association in Min protein interactions.

ABSTRACT: Division site placement in Escherichia coli involves 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 cytochrome b(5). The chimeric proteins differing in their membrane-targeting sequences were then used to establish the roles of membrane association and specificity of the membran

SUBMITTER: Taghbalout A 

PROVIDER: S-EPMC1446990 | biostudies-literature | 2006 Apr

REPOSITORIES: biostudies-literature