Super-resolution imaging and tracking of protein–protein interactions in sub-diffraction cellular space

Citations Over TimeTop 10% of 2014 papers

Abstract

Imaging the location and dynamics of individual interacting protein pairs is essential but often difficult because of the fluorescent background from other paired and non-paired molecules, particularly in the sub-diffraction cellular space. Here we develop a new method combining bimolecular fluorescence complementation and photoactivated localization microscopy for super-resolution imaging and single-molecule tracking of specific protein-protein interactions. The method is used to study the interaction of two abundant proteins, MreB and EF-Tu, in Escherichia coli cells. The super-resolution imaging shows interesting distribution and domain sizes of interacting MreB-EF-Tu pairs as a subpopulation of total EF-Tu. The single-molecule tracking of MreB, EF-Tu and MreB-EF-Tu pairs reveals intriguing localization-dependent heterogonous dynamics and provides valuable insights to understanding the roles of MreB-EF-Tu interactions.

Related Papers

• → MreB, the cell shape‐determining bacterial actin homologue, co‐ordinates cell wall morphogenesis in Caulobacter crescentus(2004)424 cited
• → Relation between rotation of MreB actin and cell width of Escherichia coli(2018)13 cited
• → Mechanical Control of Bacterial Cell Shape(2011)5 cited
• → RodZ modulates geometric localization of the bacterial actin MreB to regulate cell shape(2017)3 cited
• → Cell Size Regulation Through Tunable Geometric Localization of the Bacterial Actin Cytoskeleton(2018)1 cited