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Cell. 2016 Jul 28;166(3):637-650. doi: 10.1016/j.cell.2016.06.051.

Amyloid-like Self-Assembly of a Cellular Compartment.

Author information

1
Department of Systems Biology, Harvard Medical School, Boston, MA 02115, USA. Electronic address: elvan_boke@hms.harvard.edu.
2
Max Planck Institute of Molecular Cell Biology and Genetics, 01307 Dresden, Germany.
3
Department of Systems Biology, Harvard Medical School, Boston, MA 02115, USA; Department of Cell Biology, Harvard Medical School, Boston, MA 02115, USA.
4
Department of Systems Biology, Harvard Medical School, Boston, MA 02115, USA.
5
Department of Cell Biology, Harvard Medical School, Boston, MA 02115, USA.

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.

KEYWORDS:

velo1

PMID:
27471966
PMCID:
PMC5082712
DOI:
10.1016/j.cell.2016.06.051
[Indexed for MEDLINE]
Free PMC Article

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