Formation of subcellular compartments by condensation-prone protein OsJAZ2 in Oryza sativa and Nicotiana benthamiana leaf cells

概要

Eukaryotic cells contain membrane-less organelles consisting of proteins and other biomolecules,
which are also called biomolecular condensates, coacervates, bodies, granules, paraspeckles, or
droplets (Courchaine et al. 2016; Banani et al. 2017; Shin and Brangwynne 2017). Membrane-less
organelles form various compartments, including nucleoli, stress granules, and processing bodies,
which allow specific molecule enrichment, efficient biochemical reaction, biomolecule storage,
inhibitory substance compartmentation, and protein turnover regulation (Courchaine et al. 2016;
Banani et al. 2017; Shin and Brangwynne 2017; Franzmann et al. 2018; Pancsa et al. 2019). These
compartments are often formed by liquid–liquid phase separation, depending on the concentration, pH,
and temperature. Moreover, some condensates formed by liquid–liquid phase separation can also adopt
solid or gel-like states (Kroschwald et al. 2015; Lin et al. 2015; Banani et al. 2017; Shin and
Brangwynne 2017; Woodruff et al. 2017, 2018; Alberti et al. 2019; Bose et al. 2022). Membrane-less
organelles will be potentially useful in bioengineering and synthetic biology because they will create
platforms to modify cell function by providing an orthogonal reaction system or native protein
sequestration (Reinkemeier et al. 2019; Garabedian et al. 2021; Hastings and Boeynaems 2021).
Proteins that play an important role in liquid–liquid phase separation often contain
intrinsically disordered regions (IDRs), low-complexity domains (LCDs), or prion-like domains
(PrLDs) (Kato et al. 2012; Hennig et al. 2015; Lin et al. 2015; Molliex et al. 2015; Patel et al. 2015;
Courchaine et al. 2016; Hughes et al. 2018). Multivalent, weak non-covalent interactions between
intrinsically disordered proteins (IDPs), protein–protein interactions between folded domains, and, in
some cases, with other biomolecules such as nucleic acids, create a driving force for biological phase
separation, condensing the proteins (Banani et al. 2017; Gomes and Shorter 2019; Alberti et al. 2019). ...

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