Cryptic amyloidogenic regions in intrinsically disordered proteins
The amyloid conformation is considered a fundamental state of proteins and the propensity to populate it a generic property of polypeptides. Multiple proteome-wide analyses addressed the presence of amyloidogenic regions in proteins, nurturing our understanding of their nature and biological implica...
| Autores: | , , , |
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| Tipo de documento: | artigo |
| Data de publicação: | 2021 |
| País: | España |
| Recursos: | Universitat Autònoma de Barcelona |
| Repositório: | Dipòsit Digital de Documents de la UAB |
| Idioma: | inglês |
| OAI Identifier: | oai:ddd.uab.cat:249573 |
| Acesso em linha: | https://ddd.uab.cat/record/249573 https://dx.doi.org/urn:doi:10.1016/j.csbj.2021.07.019 |
| Access Level: | Acceso aberto |
| Palavra-chave: | Amyloid Aggregation Protein disorder Intrinsically disordered proteins Protein-protein interactions Evolution APR, Aggregation-prone region CARs, Cryptic amyloidogenic regions CD, Circular dichroism CR, Congo red FTIR, Fourier transform infrared IDPs, Intrinsically disordered proteins IDRs, Intrinsically disordered regions PBS, Phosphate buffer saline PPI, Protein-protein interactions TEM, Transmission electron microscopy Th-T, Thioflavin-T Rb, Retinoblastoma associated proteins RbC, Core region of Rb |
| Resumo: | The amyloid conformation is considered a fundamental state of proteins and the propensity to populate it a generic property of polypeptides. Multiple proteome-wide analyses addressed the presence of amyloidogenic regions in proteins, nurturing our understanding of their nature and biological implications. However, these analyses focused on highly aggregation-prone and hydrophobic stretches that are only marginally found in intrinsically disordered regions (IDRs). Here, we explore the prevalence of cryptic amyloidogenic regions (CARs) of polar nature in IDRs. CARs are widespread in IDRs and associated with IDPs function, with particular involvement in protein-protein interactions, but their presence is also connected to a risk of malfunction. By exploring this function/malfunction dichotomy, we speculate that ancestral CARs might have evolved into functional interacting regions playing a significant role in protein evolution at the origins of life. |
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