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How does ionizing radiation affect amyloidogenesis in plants?

Maryna Kryvokhyzha1,2, Sergii Litvinov1, Maksym Danchenko2

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|March 26, 2024
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Summary
This summary is machine-generated.

Ionizing radiation exposure in pea seeds triggers the accumulation of prion-like proteins, influencing plant growth and accelerating senescence. This study reveals novel insights into plant stress responses and protein remodeling.

Keywords:
Abiotic stressFTIRamyloid aggregatespisum sativumprion-like proteinsproteome

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Area of Science:

  • Plant Biology
  • Proteomics
  • Radiation Biology

Background:

  • Ionizing radiation is a significant environmental stressor that can induce plant senescence.
  • Plant senescence involves proteome remodeling, with a hypothesis that prion-like protein accumulation plays a role.
  • Pea (Pisum sativum L.) is an agriculturally important legume, yet the functional significance of its amyloidogenic proteins remains unexplored.

Purpose of the Study:

  • To investigate the impact of X-ray irradiation on pea seed germination, seedling development, and senescence.
  • To examine radiation-induced changes in protein secondary structure and the presence of amyloid aggregates.
  • To identify and functionally characterize radiation-responsive proteins, particularly putative prion-like proteins, in pea seedlings.

Main Methods:

  • Pea seeds were exposed to X-rays (5-50 Gy).
  • Fourier-transform infrared spectroscopy (FTIR) analyzed protein secondary structures (amide I/II ratio).
  • Congo red staining detected amyloid aggregates; ultrahigh-performance liquid chromatography coupled with tandem mass spectrometry (UHPLC-MS) profiled detergent-resistant proteomes. MapMan and PLAAC tools were used for functional and prion-like protein analysis.

Main Results:

  • Irradiation at 50 Gy reduced germination but increased plant height and accelerated reproductive organ development.
  • Increased beta-sheets and amyloid aggregates were observed in roots of irradiated seedlings.
  • Proteomic analysis identified 531 proteins in the detergent-resistant fraction, including 45 putative prion-like proteins. 29 proteins were differentially abundant, involved in metabolism, cytoskeleton, regulation, biosynthesis, and RNA processing.

Conclusions:

  • Protein accumulation, particularly prion-like proteins, stimulated growth, accelerated ontogenesis, and senescence, primarily via translation and RNA processing.
  • Increased primary metabolism proteins indicate heightened metabolic activity in response to X-ray exposure.
  • Further studies are needed to validate the functional role of identified amyloidogenic proteins.