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Complex of Chaperonin GroEL–α-synuclein Resolved by Cryo-EM

The accumulation of aggregated proteins causes neurodegenerative disorders, including Parkinson's, Alzheimer's, and prion diseases [1]. One cellular system designed to promote protein folding and prevent aggregation is the chaperone system, the modulation of its activity could prove to be a new approach for treatment of such diseases [2]. However, the interaction of the amyloidogenic protein with a chaperone can block the chaperone’s ability of restoring the functional state of a substrate, as shown for the ovine prion protein PrP and the GroEL chaperonin [3]. Moreover, chaperonins of gut microbiota may be involved in pathological protein transformation in the gastrointestinal tract and the subsequent prion-like spread of infectious protein forms. For instance, fibrillar forms of α-synuclein can be transported from the gut to the brain, leading to the development of Parkinson's disease [4]. Thus, structural and functional studies of interactions between amyloidogenic proteins and chaperones can assist in exploring the onset of neurodegenerative disorders. Previously, using cryo-EM, we obtained the structure of the GroEL-PrP complex and studied it using the molecular dynamics simulations [5]. Here, we present the cryo-EM structure of a complex between GroEL and α-synuclein. Recombinant human wild-type α-synuclein was produced in E. coli BL21(DE3) and GroEL was