Amyloid-like self-assembly of a cellular compartment

• Elvan Boke ; Martine Ruer ^[2] ; Martin Wühr ^[1]
  1. [1] Harvard Medical School

     Harvard Medical School

     City of Boston, Estados Unidos

     
  2. [2] Max Planck Institute
• Localización: Cell, ISSN 0092-8674, Vol. 166, Nº. 3, 2016, págs. 637-650
• Idioma: inglés
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• Resumen

  • Most vertebrate oocytes contain a Balbiani body, a large, non-membrane-bound compartment packed with RNA, mitochondria, and other organelles. Little is known about this compartment, though it specifies germline identity in many non-mammalian vertebrates. We show Xvelo, a disordered protein with an N-terminal prion-like domain, is an abundant constituent of Xenopus Balbiani bodies. Disruption of the prion-like domain of Xvelo, or substitution with a prion-like domain from an unrelated protein, interferes with its incorporation into Balbiani bodies in vivo. Recombinant Xvelo forms amyloid-like networks in vitro. Amyloid-like assemblies of Xvelo recruit both RNA and mitochondria in binding assays. We propose that Xenopus Balbiani bodies form by amyloid-like assembly of Xvelo, accompanied by co-recruitment of mitochondria and RNA. Prion-like domains are found in germ plasm organizing proteins in other species, suggesting that Balbiani body formation by amyloid-like assembly could be a conserved mechanism that helps oocytes function as long-lived germ cells.