The Disordered C-Terminus of Yeast Hsf1 Contains a Cryptic Low-Complexity Amyloidogenic Region
Response mechanisms to external stress rely on networks of proteins able to activate specific signaling pathways to ensure the maintenance of cell proteostasis. Many of the proteins mediating this kind of response contain intrinsically disordered regions, which lack a defined structure, but still ar...
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doaj-8e7ed30bcfd643588e936f17c78c5e862020-11-24T21:48:55ZengMDPI AGInternational Journal of Molecular Sciences1422-00672018-05-01195138410.3390/ijms19051384ijms19051384The Disordered C-Terminus of Yeast Hsf1 Contains a Cryptic Low-Complexity Amyloidogenic RegionJordi Pujols0Jaime Santos1Irantzu Pallarès2Salvador Ventura3Institut de Biotecnologia i de Biomedicina, Universitat Autònoma de Barcelona, E-08193 Bellaterra (Barcelona), SpainInstitut de Biotecnologia i de Biomedicina, Universitat Autònoma de Barcelona, E-08193 Bellaterra (Barcelona), SpainInstitut de Biotecnologia i de Biomedicina, Universitat Autònoma de Barcelona, E-08193 Bellaterra (Barcelona), SpainInstitut de Biotecnologia i de Biomedicina, Universitat Autònoma de Barcelona, E-08193 Bellaterra (Barcelona), SpainResponse mechanisms to external stress rely on networks of proteins able to activate specific signaling pathways to ensure the maintenance of cell proteostasis. Many of the proteins mediating this kind of response contain intrinsically disordered regions, which lack a defined structure, but still are able to interact with a wide range of clients that modulate the protein function. Some of these interactions are mediated by specific short sequences embedded in the longer disordered regions. Because the physicochemical properties that promote functional and abnormal interactions are similar, it has been shown that, in globular proteins, aggregation-prone and binding regions tend to overlap. It could be that the same principle applies for disordered protein regions. In this context, we show here that a predicted low-complexity interacting region in the disordered C-terminus of the stress response master regulator heat shock factor 1 (Hsf1) protein corresponds to a cryptic amyloid region able to self-assemble into fibrillary structures resembling those found in neurodegenerative disorders.http://www.mdpi.com/1422-0067/19/5/1384amyloidHsf1protein aggregationintrinsically disordered regionsQ/N-rich regionslow complexitymolecular recognition features |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Jordi Pujols Jaime Santos Irantzu Pallarès Salvador Ventura |
spellingShingle |
Jordi Pujols Jaime Santos Irantzu Pallarès Salvador Ventura The Disordered C-Terminus of Yeast Hsf1 Contains a Cryptic Low-Complexity Amyloidogenic Region International Journal of Molecular Sciences amyloid Hsf1 protein aggregation intrinsically disordered regions Q/N-rich regions low complexity molecular recognition features |
author_facet |
Jordi Pujols Jaime Santos Irantzu Pallarès Salvador Ventura |
author_sort |
Jordi Pujols |
title |
The Disordered C-Terminus of Yeast Hsf1 Contains a Cryptic Low-Complexity Amyloidogenic Region |
title_short |
The Disordered C-Terminus of Yeast Hsf1 Contains a Cryptic Low-Complexity Amyloidogenic Region |
title_full |
The Disordered C-Terminus of Yeast Hsf1 Contains a Cryptic Low-Complexity Amyloidogenic Region |
title_fullStr |
The Disordered C-Terminus of Yeast Hsf1 Contains a Cryptic Low-Complexity Amyloidogenic Region |
title_full_unstemmed |
The Disordered C-Terminus of Yeast Hsf1 Contains a Cryptic Low-Complexity Amyloidogenic Region |
title_sort |
disordered c-terminus of yeast hsf1 contains a cryptic low-complexity amyloidogenic region |
publisher |
MDPI AG |
series |
International Journal of Molecular Sciences |
issn |
1422-0067 |
publishDate |
2018-05-01 |
description |
Response mechanisms to external stress rely on networks of proteins able to activate specific signaling pathways to ensure the maintenance of cell proteostasis. Many of the proteins mediating this kind of response contain intrinsically disordered regions, which lack a defined structure, but still are able to interact with a wide range of clients that modulate the protein function. Some of these interactions are mediated by specific short sequences embedded in the longer disordered regions. Because the physicochemical properties that promote functional and abnormal interactions are similar, it has been shown that, in globular proteins, aggregation-prone and binding regions tend to overlap. It could be that the same principle applies for disordered protein regions. In this context, we show here that a predicted low-complexity interacting region in the disordered C-terminus of the stress response master regulator heat shock factor 1 (Hsf1) protein corresponds to a cryptic amyloid region able to self-assemble into fibrillary structures resembling those found in neurodegenerative disorders. |
topic |
amyloid Hsf1 protein aggregation intrinsically disordered regions Q/N-rich regions low complexity molecular recognition features |
url |
http://www.mdpi.com/1422-0067/19/5/1384 |
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