Document Type
Article
Publication Date
7-6-2022
Department
Biology
Abstract
To deal with increasingly severe periods of dehydration related to global climate change, it becomes increasingly important to understand the complex strategies many organisms have developed to cope with dehydration and desiccation. While it is undisputed that late embryogenesis abundant (LEA) proteins play a key role in the tolerance of plants and many anhydrobiotic organisms to water limitation, the molecular mechanisms are not well understood. In this review we recap the current knowledge of the physiological roles of LEA proteins and discuss their potential molecular functions. As these are ultimately linked to conformational changes in the presence of binding partners, posttranslational modifications or water deprivation, we give a detailed summary of the current knowledge on the structure-function relationship of LEA proteins, including their disordered state in solution, coil-to-helix transitions, self-assembly and their recently discovered ability to undergo liquid-liquid phase separation (LLPS). We point out the promising potential of LEA proteins in biotechnological and agronomic applications and summarize recent advances. We identify the most relevant open questions and discuss major challenges in establishing a solid understanding of how these intriguing molecules accomplish their tasks as cellular sentinels at the limits of surviving water scarcity.
ThinkIR Citation
Hernandez-Sanchez, Itzell E.; Lopez, Israel Maruri; Martinez-Martinez, Coral; Janis, Brett; Jimenez Bremont, Juan Francisco; Covarrubias, Alejandra A.; Menze, Michael A.; Graether, Steffen P.; and Thalhammer, Anja, "LEAfing through literature: Late embryogenesis abundant proteins coming of age – achievements and perspectives" (2022). Faculty and Staff Scholarship. 779.
https://ir.library.louisville.edu/faculty/779
DOI
10.1093/jxb/erac293
ORCID
0000-0003-1072-5462
Comments
This is a pre-copyedited, author-produced version of an article accepted for publication in Journal of Experimental Biology following peer review.
The version of record is available online at: https://doi.org/10.1093/jxb/erac293