Scientists from Martinsried and Göttingen have analyzed protein folding helpers, so-called chaperonin complexes, in their natural environment using cryo-electron tomography.
Cryo-electron tomography, or cryo-ET for short, can be used to visualize and analyze cellular structures in their natural environment. Researchers at the Max Planck Institute of Biochemistry (MPIB) in Martinsried near Munich and the University Medical Center Göttingen have now used cryo-ET to study protein folding helpers, so-called chaperonin complexes, in the bacterium Escherichia coli. These chaperonins help newly synthesized proteins to fold into their correct, functional form. The researchers were able to illuminate the folding reaction with unprecedented detail, monitoring conformational changes in the chaperonin as well as its interactions with the client protein inside the folding chambers. The results have been published in the journal Nature.
In order to gain a better understanding of how chaperonins work, Biochemist F.-Ulrich Hartl (Director at the MPI of Biochemistry) collaborated with the structural biologists Wolfgang Baumeister, Emeritus Director and inventor of cryo-ET at MPIB, and Rubén Fernández-Busnadiego from the Institute of Neuropathology at the University Medical Center Göttingen (UMG) and member of the Cluster of Excellence “Multiscale Bioimaging: From Molecular Machines to Networks of Excitable Cells” (MBExC).
