Researchers from the University of Sussex have determined the structure of nanomachine R2TP-TTT, which acts as a molecular chaperone to assemble others in the human cell. The team used cryo-electron microscopy (cryoEM) to build a detailed image of the nanomachine that shows the arrangement of all the proteins. The findings were published in Cell Reports.
Their study also reveals how the TTT proteins control the R2TP machine to allow it to hold components of mTORC1 ready for assembly. The scientists made and purified all the proteins using an insect cell system, and applied them in an ultra-thin layer that could be frozen in liquid ethane to preserve their atomic structure.
Their gathered images of the frozen protein particles were magnified more than 50,000 times and collected on cryo-electron microscopes. These were then combined using a technology related to medical tomography, to give the final detailed image of the R2TP-TTT, in which the molecular detail could be seen and analyzed.
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Laurence Pearl, one of the lead researchers said, "Previously we've been able to work out the structures of protein molecules, using a technique called X-ray crystallography, but usually only individually or in pieces. The revolution in cryoEM technology over the last couple of years has given us the ability to look at the large assemblies of proteins as they actually exist in the cell, and really understand how they work as biological nanomachines."