Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2828605 | Journal of Structural Biology | 2013 | 5 Pages |
Abstract
Affinity grids (AG) are specialized EM grids that bind macromolecular complexes containing tagged proteins to obtain maximum occupancy for structural analysis through single-particle EM. In this study, utilizing AG, we show that His-tagged activated PKC βII binds to the small ribosomal subunit (40S). We reconstructed a cryo-EM map which shows that PKC βII interacts with RACK1, a seven-bladed β-propeller protein present on the 40S and binds in two different regions close to blades 3 and 4 of RACK1. This study is a first step in understanding the molecular framework of PKC βII/RACK1 interaction and its role in translation.
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Authors
Gyanesh Sharma, Jesper Pallesen, Sanchaita Das, Robert Grassucci, Robert Langlois, Cheri M. Hampton, Deborah F. Kelly, Amedee des Georges, Joachim Frank,