Direct monitoring of interaction between Escherichia coli proteins, MinC and monomeric FtsZ, in solution.
Direct monitoring of interaction between Escherichia coli proteins, MinC and monomeric FtsZ, in solution.
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DOI：
10.1248/bpb.32.1473
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发表时间：
2009-08
影响因子：
2
通讯作者：
T. Okuno;Machiko Ogoh;Hiromitsu Tanina;N. Funasaki;K. Kogure
中科院分区：
文献类型：
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作者：
T. Okuno;Machiko Ogoh;Hiromitsu Tanina;N. Funasaki;K. Kogure
MinC在大肠杆菌细胞分裂位点的调控中起重要作用。以前的研究使用沉降和电子显微镜的方法表明，MinC与FtsZ聚合物相互作用，并抑制进一步的FtsZ聚合。然而，通过这种静态分析方法很难阐明关于特定分子相互作用的细节。在这项研究中，荧光共振能量转移（FRET）的方法，直接观察Cy3标记的MinC和Cy5标记的FtsZ在溶液中的相互作用。FRET分析表明，MinC在溶液中与单体而不是聚合物FtsZ相互作用。这表明单体FtsZ和MinC之间的相互作用对于通过MinC控制FtsZ聚合是重要的。
MinC plays an important role in regulation of the cell division site in Escherichia coli. Previous studies using sedimentation and electron microscopic methods suggested that MinC interacts with the FtsZ polymer and inhibits further FtsZ polymerization. However, it is difficult to clarify details regarding specific molecular interactions by such static analytic methods. In this study, a fluorescence resonance energy transfer (FRET) method was developed to directly observe the interaction between Cy3-labeled MinC and Cy5-labeled FtsZ in solution. FRET analysis indicated that MinC interacts with monomeric rather than polymeric FtsZ in solution. This suggests that interactions between monomeric FtsZ and MinC are important for controlling of FtsZ polymerization by MinC.