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Coordination of RNA and protein condensation by the P granule protein MEG-3
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ABSTRACT
Germ granules are RNA-protein condensates in germ cells. The mechanisms that drive germ granule assembly are not fully understood. MEG-3 is an intrinsically-disordered protein required for germ (P) granule assembly in
C. elegans
. MEG-3 forms gel-like condensates on liquid condensates assembled by PGL proteins. MEG-3 is related to the GCNA family and contains an N-terminal disordered region (IDR) and a predicted ordered C-terminus featuring an HMG-like motif (HMGL). Using
in vitro
and
in vivo
experiments, we find the MEG-3 C-terminus is necessary and sufficient to build MEG-3/PGL co-condensates independent of RNA. The HMGL domain is required for high affinity MEG-3/PGL binding
in vitro
and for assembly of MEG-3/PGL co-condensates
in vivo
. The MEG-3 IDR binds RNA
in vitro
and is required but not sufficient to recruit RNA to P granules. Our findings suggest that P granule assembly depends in part on protein-protein interactions that drive condensation independent of RNA.
Title: Coordination of RNA and protein condensation by the P granule protein MEG-3
Description:
ABSTRACT
Germ granules are RNA-protein condensates in germ cells.
The mechanisms that drive germ granule assembly are not fully understood.
MEG-3 is an intrinsically-disordered protein required for germ (P) granule assembly in
C.
elegans
.
MEG-3 forms gel-like condensates on liquid condensates assembled by PGL proteins.
MEG-3 is related to the GCNA family and contains an N-terminal disordered region (IDR) and a predicted ordered C-terminus featuring an HMG-like motif (HMGL).
Using
in vitro
and
in vivo
experiments, we find the MEG-3 C-terminus is necessary and sufficient to build MEG-3/PGL co-condensates independent of RNA.
The HMGL domain is required for high affinity MEG-3/PGL binding
in vitro
and for assembly of MEG-3/PGL co-condensates
in vivo
.
The MEG-3 IDR binds RNA
in vitro
and is required but not sufficient to recruit RNA to P granules.
Our findings suggest that P granule assembly depends in part on protein-protein interactions that drive condensation independent of RNA.
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