Structural Biology

Dynamic fibrils drive protein assembly

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Science  11 May 2018:
Vol. 360, Issue 6389, pp. 616-617
DOI: 10.1126/science.360.6389.616-f

A low-complexity domain of the protein FUS plays a role in forming RNA granules. Luo et al. identify and structurally characterize two reversible amyloid cores (RACs) in this domain. In stable amyloid fibrils, β-strands stack to form β-sheets that pack tightly and exclude water. In contrast, RAC1 forms a kinked coil that stacks along the fibril axis; two such layers interact through tyrosine ring stacking. RAC2 forms β-sheets, but with water molecules between mating sheets. It is already established that the LARK (low-complexity amyloid-like kinked segment) may be broadly involved in membraneless assemblies. The RAC2 structure suggests that reversible fibril formation may occur without kinking.

Nat. Struct. Mol. Biol. 25, 341 (2018).

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