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Seminar: Hetero-typic interactions in the aggregated state: a new kingdom beyond the RIP?
Wednesday, 21. April 2021, 12:00

Self-assembly is a fundamental foundation of life, but what about co-assembly?

Self-assembly is a fundamental foundation of life, but what about co-assembly? Many proteins that function as monomers undergo conformational transitions to self-assemble into high molecular weight polymers, and we still do not know how this “polymerizing” behaviour is encoded within their amino acid sequences. We also do not know how the same sequence is programmed to adopt different assembled forms (what I call an assembled foldome). For example, grave diseases like Amyotrophic Lateral Sclerosis (ALS) or “LATE” dementia are reportedly caused by the accumulation of different assembled forms from the same protein, named TDP-43.

Amyloids were assumed to be assembled by one type of protein, but our recent elucidation of the first 1:1 hetero-amyloid assembled by two (RIP) proteins suggests that amyloids composed of two distinct proteins playing key roles in health and disease may be common. In fact, a viral protein can displace one partner to form a distinct 1:1 hetero-amyloid that has an absolutely distinct functionality. Taking a leaf from the viral playbook, this means that for a given self-assembling sequence there may be a mating sequence driving the preferential 1:1 coassembly of the two. Thus, understanding what drives the preferential formation of coassembled forms over conventional self-assembled species will afford a new vision on assembly processes transversal to other fields of knowledge. In this talk, I will review state of the art methods and new approaches that we develop in our group to the study of self- and co-assembly processes in real time and at high resolution.

Fecha del seminario: 21/04/2021 12:00

Lugar del seminario: https://bit.ly/3toRvB8

Lugar del seminario: http://directo.csic.es/emision/iqfr

Ponente del seminario: Miguel Mompeán

Abstract