Luminidependens (LD) is an Arabidopsis protein with prion behavior

Sohini Chakrabortee, Can Kayatekin, Greg A. Newby, Marc L. Mendillo, Alex Lancaster, Susan Lindquist*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

67 Scopus citations

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 higherorder assemblies. For most yeast prions, the capacity to convert into a prion resides in a distinct prion domain. Thus, new prionforming 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.

Original languageEnglish (US)
Pages (from-to)6065-6070
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume113
Issue number21
DOIs
StatePublished - May 24 2016

Keywords

  • Luminidependens
  • Plant prion domains
  • Prions

ASJC Scopus subject areas

  • General

Fingerprint Dive into the research topics of 'Luminidependens (LD) is an Arabidopsis protein with prion behavior'. Together they form a unique fingerprint.

Cite this