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

Ginsawaeng, O., Heise, C., Sangwan, R., Karcher, D., Hernández-Sánchez, I., Sampathkumar, A., et al. (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(12): 1770. doi:10.3390/biom11121770.

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Ginsawaeng, O.1, Author              
Heise, C.1, Author              
Sangwan, R.2, Author              
Karcher, D.2, Author              
Hernández-Sánchez, I.E.1, Author              
Sampathkumar, A.3, Author              
Zuther, E.1, Author              
Affiliations:
1Transcript Profiling, Infrastructure Groups and Service Units, Max Planck Institute of Molecular Plant Physiology, Max Planck Society, ou_1753306              
2Organelle Biology and Biotechnology, Department Bock, Max Planck Institute of Molecular Plant Physiology, Max Planck Society, ou_1753326              
3Plant Cell Biology and Microscopy, Infrastructure Groups and Service Units, Max Planck Institute of Molecular Plant Physiology, Max Planck Society, ou_2253647              

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 Abstract: 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.

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Language(s): eng - English
 Dates: 2021-11-25
 Publication Status: Published in print
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 Identifiers: DOI: 10.3390/biom11121770
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Title: Biomolecules
Source Genre: Journal
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Publ. Info: Basel, Switzerland : MDPI
Pages: - Volume / Issue: 11 (12) Sequence Number: 1770 Start / End Page: - Identifier: ISSN: 2218-273X
CoNE: https://pure.mpg.de/cone/journals/resource/2218-273X