【摘 要】
：
Imaging localization and dynamics of individual interacting protein pairs is essential but often difficult due to the fluorescent background from other paired and non-paired molecules,particularly in
【机 构】
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State Key Laboratory of Biomembrane and Membrane Biotechnology,Biodynamic Optical Imaging Center (BI
【出 处】
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中国化学会第三届全国生物物理化学会议暨国际华人生物物理化学发展论坛
论文部分内容阅读
Imaging localization and dynamics of individual interacting protein pairs is essential but often difficult due to the fluorescent background from other paired and non-paired molecules,particularly in the sub-diffraction cellular space.Here based on split mEos3.2,we developed a new method combining Bimolecular Fluorescence Complementation (BiFC) and Photoactivated Localization Microscopy (PALM)for super-resolution imaging and tracking of specific protein-protein interactions.The method was used to study the interaction of two abundant proteins,MreB and EF-Tu,in Escherichia coli cells.The super-resolution imaging showed interesting distribution and domain sizes of interacting MreB-EF-Tu pairs as a subpopulation of total EF-Tu.The super-resolution single molecule tracking of MreB,EF-Tu,and MreB-EF-Tu pairs revealed intriguing localization-dependent heterogonous dynamics and provided valuable insights to understanding the roles of MreB-EF-Tu interactions.
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