Exploring cryptic amyloidogenic regions in prion-like proteins from plants

Area of Science:

• Biochemistry
• Molecular Biology
• Bioinformatics

Background:

• Prion-like domains (PrLDs) are intrinsically disordered regions (IDRs) found in proteins across various organisms.
• These domains share compositional similarities with yeast prion domains and are implicated in regulatory processes.
• Certain regions within IDRs, termed cryptic amyloidogenic regions (CARs), possess moderate amyloid propensity and can self-assemble into fibrils.

Purpose of the Study:

• To identify and characterize CARs in plant prion-like proteins (pCARs).
• To investigate the evolutionary conservation and functional significance of pCARs.
• To analyze the compositional bias of pCARs in plants, a less-studied lineage.

Main Methods:

• Bioinformatic analysis to identify CARs in plant prion-like proteins.
• Experimental validation of the amyloid potential of a selected pCAR from *Arabidopsis thaliana*.
• Functional enrichment analysis and compositional bias assessment of pCARs.

Main Results:

• Thousands of predicted CARs were identified in plant prion-like proteins.
• A selected pCAR from *Arabidopsis thaliana* demonstrated intrinsic amyloid-forming potential.
• pCARs exhibit evolutionary conservation and specific compositional biases within plant prion-like proteins.

Conclusions:

• Cryptic amyloidogenic regions are present and conserved in plant prion-like proteins.
• These regions contribute to the functional roles of plant prion-like proteins.
• The study provides insights into the understudied plant prionome and the role of IDRs in protein function.