| Autor: |
Shattuck JE; a Department of Biochemistry and Molecular Biology , Colorado State University , Fort Collins , CO , USA., Waechter AC; a Department of Biochemistry and Molecular Biology , Colorado State University , Fort Collins , CO , USA., Ross ED; a Department of Biochemistry and Molecular Biology , Colorado State University , Fort Collins , CO , USA. |
| Jazyk: |
angličtina |
| Zdroj: |
Prion [Prion] 2017 Jul 04; Vol. 11 (4), pp. 249-264. Date of Electronic Publication: 2017 Jun 30. |
| DOI: |
10.1080/19336896.2017.1344806 |
| Abstrakt: |
Prion-like domains are low complexity, intrinsically disordered domains that compositionally resemble yeast prion domains. Many prion-like domains are involved in the formation of either functional or pathogenic protein aggregates. These aggregates range from highly dynamic liquid droplets to highly ordered detergent-insoluble amyloid-like aggregates. To better understand the amino acid sequence features that promote conversion to stable, detergent-insoluble aggregates, we used the prediction algorithm PAPA to identify predicted aggregation-prone prion-like domains with a range of compositions. While almost all of the predicted aggregation-prone domains formed foci when expressed in cells, the ability to form the detergent-insoluble aggregates was highly correlated with glutamine/asparagine (Q/N) content, suggesting that high Q/N content may specifically promote conversion to the amyloid state in vivo. We then used this data set to examine cross-seeding between prion-like proteins. The prion protein Sup35 requires the presence of a second prion, [PIN + ], to efficiently form prions, but this requirement can be circumvented by the expression of various Q/N-rich protein fragments. Interestingly, almost all of the Q/N-rich domains that formed SDS-insoluble aggregates were able to promote prion formation by Sup35, highlighting the highly promiscuous nature of these interactions. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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