TY - JOUR
T1 - Amyloid-like Self-Assembly of a Cellular Compartment
AU - Boke, Elvan
AU - Ruer, Martine
AU - Wühr, Martin
AU - Coughlin, Margaret
AU - Lemaitre, Regis
AU - Gygi, Steven P.
AU - Alberti, Simon
AU - Drechsel, David
AU - Hyman, Anthony A.
AU - Mitchison, Timothy J.
N1 - Funding Information:
We thank members of the T.J.M. and A.A.H. labs, especially Avinash Patel for helpful discussions, Andrei Pozniakovski for cloning, and Christine Field for help in making extracts. We would like to thank Doris Richter and Sonja Kroschwald for technical assistance. We are grateful to the Protein Expression, Electron Microscopy and Image Processing facilities of the MPI-CBG for their support. We would also like to thank the Nikon Imaging Center at Harvard Medical School for microscopy support. Proteomic analysis was supported by NIH grant R01-GM103785 (PI Marc W. Kirschner). M.W. was supported by the Charles A. King Trust Postdoctoral Fellowship. This work was supported by the MaxSynBio consortium, which is jointly funded by the Federal Ministry of Education and Research of Germany and the Max Planck Society (to A.A.H.) and NIH grant GM39565 (to T.J.M.).
Publisher Copyright:
© 2016 Elsevier Inc.
PY - 2016/7/28
Y1 - 2016/7/28
N2 - 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.
AB - 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.
KW - velo1
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U2 - 10.1016/j.cell.2016.06.051
DO - 10.1016/j.cell.2016.06.051
M3 - Article
C2 - 27471966
AN - SCOPUS:84979581124
SN - 0092-8674
VL - 166
SP - 637
EP - 650
JO - Cell
JF - Cell
IS - 3
ER -