title: Amyloid-like Self-Assembly of a Cellular Compartment.
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.
authors.affiliation: Department of Systems Biology, Harvard Medical School, Boston, MA 02115, USA. Electronic address: elvan_boke@hms.harvard.edu.
authors.forename: Elvan
authors.initials: E
authors.lastname: Boke
authors.affiliation: Max Planck Institute of Molecular Cell Biology and Genetics, 01307 Dresden, Germany.
authors.forename: Martine
authors.initials: M
authors.lastname: Ruer
authors.affiliation: Department of Systems Biology, Harvard Medical School, Boston, MA 02115, USA; Department of Cell Biology, Harvard Medical School, Boston, MA 02115, USA.
authors.forename: Martin
authors.initials: M
authors.lastname: Wühr
authors.affiliation: Department of Systems Biology, Harvard Medical School, Boston, MA 02115, USA.
authors.forename: Margaret
authors.initials: M
authors.lastname: Coughlin
authors.affiliation: Max Planck Institute of Molecular Cell Biology and Genetics, 01307 Dresden, Germany.
authors.forename: Regis
authors.initials: R
authors.lastname: Lemaitre
authors.affiliation: Department of Cell Biology, Harvard Medical School, Boston, MA 02115, USA.
authors.forename: Steven P
authors.initials: SP
authors.lastname: Gygi
authors.affiliation: Max Planck Institute of Molecular Cell Biology and Genetics, 01307 Dresden, Germany.
authors.forename: Simon
authors.initials: S
authors.lastname: Alberti
authors.affiliation: Max Planck Institute of Molecular Cell Biology and Genetics, 01307 Dresden, Germany.
authors.forename: David
authors.initials: D
authors.lastname: Drechsel
authors.affiliation: Max Planck Institute of Molecular Cell Biology and Genetics, 01307 Dresden, Germany.
authors.forename: Anthony A
authors.initials: AA
authors.lastname: Hyman
authors.affiliation: Department of Systems Biology, Harvard Medical School, Boston, MA 02115, USA.
authors.forename: Timothy J
authors.initials: TJ
authors.lastname: Mitchison
mesh_terms: D000682:Amyloid / Q000378:metabolism*; D000818:Animals; D052160:Benzothiazoles; D005260:Female; D005456:Fluorescent Dyes; D008928:Mitochondria / Q000378:metabolism; D009865:Oocytes / Q000166:cytology; D001678:Organelle Biogenesis; D015388:Organelles / Q000378:metabolism; D011328:Prions / Q000737:chemistry; D000072417:Protein Domains; D021381:Protein Transport; D012333:RNA, Messenger / Q000378:metabolism; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000378:metabolism; D061987:Sf9 Cells; D020825:T-Box Domain Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D013844:Thiazoles; D029867:Xenopus Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D014982:Xenopus laevis; D015027:Zebrafish
chemical_list: D000682:Amyloid; D052160:Benzothiazoles; D005456:Fluorescent Dyes; D011328:Prions; D012333:RNA, Messenger; D011993:Recombinant Fusion Proteins; D020825:T-Box Domain Proteins; D013844:Thiazoles; D029867:Xenopus Proteins; C483179:velo1 protein, Xenopus; C009462:thioflavin T
keywords: velo1