TY - JOUR
T1 - Exploring cryptic amyloidogenic regions in prion-like proteins from plants
AU - Pintado-Grima, Carlos
AU - Santos, Jaime
AU - Iglesias, Valentín
AU - Manglano-Artuñedo, Zoe
AU - Pallarès, Irantzu
AU - Ventura, Salvador
N1 - Funding Information:
This work was funded by European Union’s Horizon 2020 research and innovation programme under GA 952334 (PhasAGE). SV was supported by the Spanish Ministry of Science and Innovation (PID 2019-105017RB-I00), by ICREA and ICREA Academia 2020. CP-G was supported by the Secretariat of Universities and Research of the Catalan Government and the European Social Fund (2021 FI_B 00087). JS was supported by the Spanish Ministry of Science and Innovation via a doctoral Grant (FPU17/01157). VI was supported by the Spanish Ministry of Universities and the European Union-Next Generation EU (ruling 02/07/2021, Universitat Autònoma de Barcelona).
Publisher Copyright:
Copyright © 2023 Pintado-Grima, Santos, Iglesias, Manglano-Artuñedo, Pallarès and Ventura.
PY - 2023/1/16
Y1 - 2023/1/16
N2 - Prion-like domains (PrLDs) are intrinsically disordered regions (IDRs) of low sequence complexity with a similar composition to yeast prion domains. PrLDs-containing proteins have been involved in different organisms’ regulatory processes. Regions of moderate amyloid propensity within IDRs have been shown to assemble autonomously into amyloid fibrils. These sequences tend to be rich in polar amino acids and often escape from the detection of classical bioinformatics screenings that look for highly aggregation-prone hydrophobic sequence stretches. We defined them as cryptic amyloidogenic regions (CARs) and recently developed an integrated database that collects thousands of predicted CARs in IDRs. CARs seem to be evolutionary conserved among disordered regions because of their potential to stablish functional contacts with other biomolecules. Here we have focused on identifying and characterizing CARs in prion-like proteins (pCARs) from plants, a lineage that has been poorly studied in comparison with other prionomes. We confirmed the intrinsic amyloid potential for a selected pCAR from Arabidopsis thaliana and explored functional enrichments and compositional bias of pCARs in plant prion-like proteins.
AB - Prion-like domains (PrLDs) are intrinsically disordered regions (IDRs) of low sequence complexity with a similar composition to yeast prion domains. PrLDs-containing proteins have been involved in different organisms’ regulatory processes. Regions of moderate amyloid propensity within IDRs have been shown to assemble autonomously into amyloid fibrils. These sequences tend to be rich in polar amino acids and often escape from the detection of classical bioinformatics screenings that look for highly aggregation-prone hydrophobic sequence stretches. We defined them as cryptic amyloidogenic regions (CARs) and recently developed an integrated database that collects thousands of predicted CARs in IDRs. CARs seem to be evolutionary conserved among disordered regions because of their potential to stablish functional contacts with other biomolecules. Here we have focused on identifying and characterizing CARs in prion-like proteins (pCARs) from plants, a lineage that has been poorly studied in comparison with other prionomes. We confirmed the intrinsic amyloid potential for a selected pCAR from Arabidopsis thaliana and explored functional enrichments and compositional bias of pCARs in plant prion-like proteins.
KW - bioinformatics
KW - cryptic amyloidogenic regions
KW - functional interactions
KW - plants
KW - prion-like domains
UR - http://www.scopus.com/inward/record.url?scp=85147157015&partnerID=8YFLogxK
UR - https://www.mendeley.com/catalogue/75799b65-c5e2-37b9-b266-2cc86872b4a1/
U2 - 10.3389/fpls.2022.1060410
DO - 10.3389/fpls.2022.1060410
M3 - Article
C2 - 36726678
AN - SCOPUS:85147157015
SN - 1664-462X
VL - 13
JO - Frontiers in Plant Science
JF - Frontiers in Plant Science
M1 - 1060410
ER -