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Plant Group II LEA Proteins: Intrinsically Disordered Structure for Multiple Functions in Response to Environmental Stresses
Article

Subcellular Localization of Seed-Expressed LEA_4 Proteins Reveals Liquid-Liquid Phase Separation for LEA9 and for LEA48 Homo- and LEA42-LEA48 Heterodimers

Max Planck Institute of Molecular Plant Physiology, Am Mühlenberg 1, 14476 Potsdam, Germany
*
Author to whom correspondence should be addressed.
Current address: Institute of Life Science, University of Rostock, Albert-Einstein-Str. 3, 18059 Rostock, Germany.
Current address: Max Planck Institute for Plant Breeding Research, Carl-von-Linne-Weg 10, 50829 Cologne, Germany.
§
Current address: Center for Desert Agriculture, Biological and Environmental Science and Engineering Division, King Abdullah University of Science and Technology (KAUST), Thuwal 23955-6900, Saudi Arabia.
Academic Editor: Steffen Graether
Biomolecules 2021, 11(12), 1770; https://doi.org/10.3390/biom11121770
Received: 27 September 2021 / Revised: 5 November 2021 / Accepted: 20 November 2021 / Published: 25 November 2021
LEA proteins are involved in plant stress tolerance. In Arabidopsis, the LEA_4 Pfam group is the biggest group with the majority of its members being expressed in dry seeds. To assess subcellular localization in vivo, we investigated 11 seed-expressed LEA_4 proteins in embryos dissected from dry seeds expressing LEA_4 fusion proteins under its native promoters with the Venus fluorescent protein (proLEA_4::LEA_4:Venus). LEA_4 proteins were shown to be localized in the endoplasmic reticulum, nucleus, mitochondria, and plastids. LEA9, in addition to the nucleus, was also found in cytoplasmic condensates in dry seeds dependent on cellular hydration level. Most investigated LEA_4 proteins were detected in 4-d-old seedlings. In addition, we assessed bioinformatic tools for predicting subcellular localization and promoter motifs of 11 seed-expressed LEA_4 proteins. Ratiometric bimolecular fluorescence complementation assays showed that LEA7, LEA29, and LEA48 form homodimers while heterodimers were formed between LEA7-LEA29 and LEA42-LEA48 in tobacco leaves. Interestingly, LEA48 homodimers and LEA42-LEA48 heterodimers formed droplets structures with liquid-like behavior. These structures, along with LEA9 cytoplasmic condensates, may have been formed through liquid-liquid phase separation. These findings suggest possible important roles of LLPS for LEA protein functions. View Full-Text
Keywords: subcellular localization; LEA_4 proteins; seed-expressed; cytoplasmic condensates; heterodimer subcellular localization; LEA_4 proteins; seed-expressed; cytoplasmic condensates; heterodimer
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MDPI and ACS Style

Ginsawaeng, O.; Heise, C.; Sangwan, R.; Karcher, D.; Hernández-Sánchez, I.E.; Sampathkumar, A.; Zuther, E. Subcellular Localization of Seed-Expressed LEA_4 Proteins Reveals Liquid-Liquid Phase Separation for LEA9 and for LEA48 Homo- and LEA42-LEA48 Heterodimers. Biomolecules 2021, 11, 1770. https://doi.org/10.3390/biom11121770

AMA Style

Ginsawaeng O, Heise C, Sangwan R, Karcher D, Hernández-Sánchez IE, Sampathkumar A, Zuther E. Subcellular Localization of Seed-Expressed LEA_4 Proteins Reveals Liquid-Liquid Phase Separation for LEA9 and for LEA48 Homo- and LEA42-LEA48 Heterodimers. Biomolecules. 2021; 11(12):1770. https://doi.org/10.3390/biom11121770

Chicago/Turabian Style

Ginsawaeng, Orarat, Carolin Heise, Rohit Sangwan, Daniel Karcher, Itzell E. Hernández-Sánchez, Arun Sampathkumar, and Ellen Zuther. 2021. "Subcellular Localization of Seed-Expressed LEA_4 Proteins Reveals Liquid-Liquid Phase Separation for LEA9 and for LEA48 Homo- and LEA42-LEA48 Heterodimers" Biomolecules 11, no. 12: 1770. https://doi.org/10.3390/biom11121770

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