'Towards understanding protein organization of membrane environments in situ using electron cryo-tomography'

Host: Liz Miller

Venue:  MSI Small Lecture Theatre, SLS

Abstract:

The recent ‘resolution revolution’ has led to a boost of protein structures solved by cryo-EM. At the same time new technical developments have led to a vibrant and quickly growing field of in situ cryo-ET. We can now study protein structure in relation to membrane ultrastructure directly in the native cellular environment. I’m going to show how we can use this technique to further our understanding of the protein organization in cellular membrane environments, such as the organization of lipid transfer proteins at endoplasmic reticulum - plasma membrane contact sites, or movements of the nuclear pore complex (NPC) scaffold during osmotic stress. The powerful combination of subtomogram averaging and systematic fitting of AlphaFold generated models allows us to build a first structural model of the Dictyostelium discoideum NPC architecture. With current in situ cryo-ET techniques, we can solve ribosomes structures to below 3.5 Å resolution and provide valuable insights in the translation elongation cycle. However, as software tools are developing further, even identification of smaller complexes becomes feasible, eventually making smaller protein targets, such as membrane transporters and channels directly accessible in cells.

 

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