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Exploring cryptic amyloidogenic regions in prion-like proteins from plants

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...

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Autores principales: Pintado-Grima, Carlos, Santos, Jaime, Iglesias, Valentín, Manglano-Artuñedo, Zoe, Pallarès, Irantzu, Ventura, Salvador
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9885169/
https://www.ncbi.nlm.nih.gov/pubmed/36726678
http://dx.doi.org/10.3389/fpls.2022.1060410
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author Pintado-Grima, Carlos
Santos, Jaime
Iglesias, Valentín
Manglano-Artuñedo, Zoe
Pallarès, Irantzu
Ventura, Salvador
author_facet Pintado-Grima, Carlos
Santos, Jaime
Iglesias, Valentín
Manglano-Artuñedo, Zoe
Pallarès, Irantzu
Ventura, Salvador
author_sort Pintado-Grima, Carlos
collection PubMed
description 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.
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spelling pubmed-98851692023-01-31 Exploring cryptic amyloidogenic regions in prion-like proteins from plants Pintado-Grima, Carlos Santos, Jaime Iglesias, Valentín Manglano-Artuñedo, Zoe Pallarès, Irantzu Ventura, Salvador Front Plant Sci Plant Science 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. Frontiers Media S.A. 2023-01-16 /pmc/articles/PMC9885169/ /pubmed/36726678 http://dx.doi.org/10.3389/fpls.2022.1060410 Text en Copyright © 2023 Pintado-Grima, Santos, Iglesias, Manglano-Artuñedo, Pallarès and Ventura https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Plant Science
Pintado-Grima, Carlos
Santos, Jaime
Iglesias, Valentín
Manglano-Artuñedo, Zoe
Pallarès, Irantzu
Ventura, Salvador
Exploring cryptic amyloidogenic regions in prion-like proteins from plants
title Exploring cryptic amyloidogenic regions in prion-like proteins from plants
title_full Exploring cryptic amyloidogenic regions in prion-like proteins from plants
title_fullStr Exploring cryptic amyloidogenic regions in prion-like proteins from plants
title_full_unstemmed Exploring cryptic amyloidogenic regions in prion-like proteins from plants
title_short Exploring cryptic amyloidogenic regions in prion-like proteins from plants
title_sort exploring cryptic amyloidogenic regions in prion-like proteins from plants
topic Plant Science
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9885169/
https://www.ncbi.nlm.nih.gov/pubmed/36726678
http://dx.doi.org/10.3389/fpls.2022.1060410
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