Abstract
Intrinsically disordered late embryogenesis abundant (LEA) proteins play a central role in the tolerance of plants and other organisms to dehydration brought upon, for example, by freezing temperatures, high salt concentration, drought or desiccation, and many LEA proteins have been found to stabilize dehydration-sensitive cellular structures. Their conformational ensembles are highly sensitive to the environment, allowing them to undergo conformational changes and adopt ordered secondary and quaternary structures and to participate in formation of membraneless organelles. In an interdisciplinary approach, we discovered how the functional diversity of the Arabidopsis thaliana LEA protein COR15A found in vitro is encoded in its structural repertoire, with the stabilization of membranes being achieved at the level of secondary structure and the stabilization of enzymes accomplished by the formation of oligomeric complexes. We provide molecular details on intra- and inter-monomeric helix–helix interactions, demonstrate how oligomerization is driven by an α-helical molecular recognition feature (α-MoRF) and provide a rationale that the formation of noncanonical, loosely packed, right-handed coiled-coils might be a recurring theme for homo- and hetero-oligomerization of LEA proteins.
| Original language | English |
|---|---|
| Article number | e4989 |
| Journal | Protein Science |
| Volume | 33 |
| Issue number | 5 |
| DOIs | |
| State | Published - May 2024 |
Funding
Many thanks to the late Dirk Hincha, whose ideas and enthusiasm powered the early steps of this project. We thank Anne Riedel for her excellent experimental help, Carlos Becerra for technical assistance during the illustration art design, Carlos Navarro-Retamal for providing Gromacs scripts and kindly sharing his experience, Arun Sampathkumar for his scientific and technical guidance and discussion with respect to confocal laser scanning microscopy and image processing and Katja Arndt for generously making the fluorescence plate reader available. We acknowledge support by the Max Planck Computing and Data Facility. M.S.M. and T.R. are supported by the Trond Mohn Foundation BFS2017TMT01. The National Deuteration Facility is partly supported by the National Collaborative Research Infrastructure Strategy\u2014an initiative of the Australian Government (deuteration proposals NDF8141 to A.M.S. and NDF6449 to C.J.G.). A portion of this research used resources at the Spallation Neutron Source, a DOE Office of Science User Facility operated by the Oak Ridge National Laboratory (neutron proposal 30279.1 to A.M.S.). Open Access funding enabled and organized by Projekt DEAL. We thank Anne Riedel for her excellent experimental help, Carlos Becerra for technical assistance during the illustration art design, Carlos Navarro\u2010Retamal for providing Gromacs scripts and kindly sharing his experience, Arun Sampathkumar for his scientific and technical guidance and discussion with respect to confocal laser scanning microscopy and image processing and Katja Arndt for generously making the fluorescence plate reader available. We acknowledge support by the Max Planck Computing and Data Facility. M.S.M. and T.R. are supported by the Trond Mohn Foundation BFS2017TMT01. The National Deuteration Facility is partly supported by the National Collaborative Research Infrastructure Strategy\u2014an initiative of the Australian Government (deuteration proposals NDF8141 to A.M.S. and NDF6449 to C.J.G.). A portion of this research used resources at the Spallation Neutron Source, a DOE Office of Science User Facility operated by the Oak Ridge National Laboratory (neutron proposal 30279.1 to A.M.S.). Open Access funding enabled and organized by Projekt DEAL.
Keywords
- freezing tolerance
- functional plasticity
- intrinsically disordered protein
- late embryogenesis abundant protein
- self-assembly