Prion-like protein found in plants

Photo of plate showing different strengths of prion activity in yeast

Whitehead Institute scientists inserted the Arabidopsis thaliana protein Luminidependens (LD) into yeast to determine whether it has the traits of a prion.  Prion variation can occur in genetically identical yeast cells.  As seen in this plate of LD-containing yeast, darker red colored streaks (labeled as 2) have weak prion activity, whereas white streaks have stronger prion activity (labeled as 4).

Image: Courtesy of PNAS

April 29, 2016

Tags: Lindquist LabProtein Function

CAMBRIDGE, Mass. (April 29, 2016) – Whitehead Institute scientists have determined that a plant protein involved in the timing of flowering could in fact be a prion. This is the first time that a possible prion has been identified in plants.

Infamous for causing fatal degenerative brain diseases, such as bovine spongiform encephalopathy, known more commonly as “mad cow disease,” Creutzfeldt-Jakob disease, and scrapie, prions are proteins that have the ability to self-perpetuate when they assume a particular conformation. They can be inherited separately from DNA.

Although prions are typically associated with negative effects, recent research from Whitehead Member Susan Lindquist’s lab has shown that prions can introduce evolutionarily beneficial traits that help an organism survive environmental stresses. Lindquist’s lab has identified such prions in yeast, including several that are able to regulate transcription, translation, and RNA processing.

“In fungi prions are highly evolved  proteins that provide a wide diversity of novel phenotype and in neurons at least one prion, CPEB, helps to perpetuate the activity state of synapses to aid long-term memory," say Lindquist, who is also a Howard Hughes Medical Institute investigator and a professor of biology at Massachusetts Institute of Technology.

In the current work, which is reported online this week in the journal PNAS, researchers in the Lindquist lab screened protein fragments from Arabidopsis thaliana, a relative of the mustard plant, and identified 474 that contain prion-like domains. Of those, the team, led by postdoctoral researcher Sohini Chakrabortee, focused on four prion candidates in the autonomous flowering pathway, which controls the timing of flowering in response to yet-unknown internal cues.

To see if the candidates have the properties of prions, the scientists inserted the proteins into yeast, a model that the Lindquist lab has studied extensively. After testing the candidates with several tools used to identify prions, the scientists determined that one of the proteins, called Luminidependens (LD), has several traits associated with prions and could maintain a heritable, self-perpetuating state.

“We weren’t surprised that a plant could have a prion. It would be more surprising if only yeast and mammals have prions and nothing else does,” says Can Kayatekin, a postdoctoral researcher who is an author of the PNAS paper. “While more work needs to be done to show these proteins do indeed function as prions in plants, clearly it is a very real possibility. We hope this work can motivate scientists to be the lookout for prions in plants.”

Greg Newby, a Lindquist graduate student and another author of the paper agrees.

“This fundamental research expands our view of where functional prions may act,” adds Newby. “I wonder how many organisms and cellular pathways may utilize prion propagation.”

 

This work was supported by Howard Hughes Medical Institute, Harold and Leila Mathers Charitable Foundation, Eleanor Schwartz Charitable Foundation, Broodbank Fund, Hughes Hall at University of Cambridge, and National Science Foundation.

 

Written by Nicole Giese Rura

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Susan Lindquist’s primary affiliation is with Whitehead Institute for Biomedical Research, where her laboratory is located and all her research is conducted. She is also a Howard Hughes Medical Institute investigator and a professor of biology at Massachusetts Institute of Technology. 

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Full Citation:

“Luminidependens (LD) is an Arabidopsis protein with prion behavior”

PNAS, online the week of April 25, 2016.

Sohini Chakrabortee (1,4), Can Kayatekin (1), Greg A. Newby (1,2), Marc L. Mendillo (1), Alex Lancaster (1,5), and Susan Lindquist (1,2,3).

1. Whitehead Institute for Biomedical Research, Cambridge, MA 02142

2. Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139

3. Howard Hughes Medical Institute, Cambridge, MA 02139

4. Present address: University of Birmingham, Edgbaston, Birmingham, B15 2TT, United Kingdom.

5. Present address: Department of Pathology, Beth Israel Deaconess Medical Center, Boston, MA 02215. 

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