Luminidependens (LD) is an Arabidopsis protein with prion behavior
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PNAS-2016-Chakrabortee-6065-70.pdf
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Author(s)
Chakrabortee, Sohini
Kayatekin, Can
Mendillo, Marc L.
Lancaster, Alex
Newby, Gregory Arthur
Lindquist, Susan
Date Issued
April 2016
Journal
Proceedings of the National Academy of Sciences
Publisher
National Academy of Sciences (U.S.)
Citation
Chakrabortee, Sohini et al. “Luminidependens (LD) Is an Arabidopsis Protein with Prion Behavior.” Proceedings of the National Academy of Sciences 113.21 (2016): 6065–6070. © 2016 National Academy of Sciences
Version
Final published version
Abstract
Prion proteins provide a unique mode of biochemical memory through self-perpetuating changes in protein conformation and function. They have been studied in fungi and mammals, but not yet identified in plants. Using a computational model, we identified candidate prion domains (PrDs) in nearly 500 plant proteins. Plant flowering is of particular interest with respect to biological memory, because its regulation involves remembering and integrating previously experienced environmental conditions. We investigated the prion-forming capacity of three prion candidates involved in flowering using a yeast model, where prion attributes are well defined and readily tested. In yeast, prions heritably change protein functions by templating monomers into higher-order assemblies. For most yeast prions, the capacity to convert into a prion resides in a distinct prion domain. Thus, new prion-forming domains can be identified by functional complementation of a known prion domain. The prion-like domains (PrDs) of all three of the tested proteins formed higher-order oligomers. Uniquely, the Luminidependens PrD (LDPrD) fully replaced the prion-domain functions of a well-characterized yeast prion, Sup35. Our results suggest that prion-like conformational switches are evolutionarily conserved and might function in a wide variety of normal biological processes.
MIT Department
Massachusetts Institute of Technology. Department of Biology
Whitehead Institute for Biomedical Research
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DOI of Published Version
https://doi.org/10.1073/pnas.1604478113
