Arabidopsis FLL2 promotes liquid–liquid phase separation of polyadenylation complexes

Xiaofeng Fang, Liang Wang, Ryo Ishikawa, Yaoxi Li, Marc Fiedler, Fuquan Liu, Grant Calder, Beth Rowan, Detlef Weigel, Pilong Li () and Caroline Dean ()
Additional contact information
Xiaofeng Fang: John Innes Centre
Liang Wang: Tsinghua University
Ryo Ishikawa: John Innes Centre
Yaoxi Li: John Innes Centre
Marc Fiedler: MRC Laboratory of Molecular Biology
Fuquan Liu: John Innes Centre
Grant Calder: John Innes Centre
Beth Rowan: Max Planck Institute for Developmental Biology
Detlef Weigel: Max Planck Institute for Developmental Biology
Pilong Li: Tsinghua University
Caroline Dean: John Innes Centre

Nature, 2019, vol. 569, issue 7755, 265-269

Abstract: Abstract An important component of cellular biochemistry is the concentration of proteins and nucleic acids in non-membranous compartments1,2. These biomolecular condensates are formed from processes that include liquid–liquid phase separation. The multivalent interactions necessary for liquid–liquid phase separation have been extensively studied in vitro1,3. However, the regulation of this process in vivo is poorly understood. Here we identify an in vivo regulator of liquid–liquid phase separation through a genetic screen targeting factors required for Arabidopsis RNA-binding protein FCA function. FCA contains prion-like domains that phase-separate in vitro, and exhibits behaviour in vivo that is consistent with phase separation. The mutant screen identified a functional requirement for FLL2, a coiled-coil protein, in the formation of FCA nuclear bodies. FCA reduces transcriptional read-through by promoting proximal polyadenylation at many sites in the Arabidopsis genome3,4. FLL2 was required to promote this proximal polyadenylation, but not the binding of FCA to target RNA. Ectopic expression of FLL2 increased the size and number of FCA nuclear bodies. Crosslinking with formaldehyde captured in vivo interactions between FLL2, FCA and the polymerase and nuclease modules of the RNA 3′-end processing machinery. These 3′ RNA-processing components colocalized with FCA in the nuclear bodies in vivo, which indicates that FCA nuclear bodies compartmentalize 3′-end processing factors to enhance polyadenylation at specific sites. Our findings show that coiled-coil proteins can promote liquid–liquid phase separation, which expands our understanding of the principles that govern the in vivo dynamics of liquid-like bodies.

Date: 2019
References: Add references at CitEc
Citations: View citations in EconPapers (2)

Downloads: (external link)
https://www.nature.com/articles/s41586-019-1165-8 Abstract (text/html)
Access to the full text of the articles in this series is restricted.

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:569:y:2019:i:7755:d:10.1038_s41586-019-1165-8

Ordering information: This journal article can be ordered from
https://www.nature.com/

DOI: 10.1038/s41586-019-1165-8

Access Statistics for this article

Nature is currently edited by Magdalena Skipper

More articles in Nature from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().