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XB-ART-52311
Cell July 28, 2016; 166 (3): 637-650.

Amyloid-like Self-Assembly of a Cellular Compartment.

Boke E , Ruer M , Wühr M , Coughlin M , Lemaitre R , Gygi SP , Alberti S , Drechsel D , Hyman AA , Mitchison TJ .


Abstract
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.

PubMed ID: 27471966
PMC ID: PMC5082712
Article link: Cell
Grant support: [+]
Genes referenced: prnp

References [+] :
Alberti, A systematic survey identifies prions and illuminates sequence features of prionogenic proteins. 2009, Pubmed


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