Amyloid Properties of the FXR1 Protein Are Conserved in Evolution of Vertebrates
Functional amyloids are fibrillary proteins with a cross-β structure that play a structural or regulatory role in pro- and eukaryotes. Previously, we have demonstrated that the RNA-binding FXR1 protein functions in an amyloid form in the rat brain. This RNA-binding protein plays an important role in...
| Main Authors: | , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
MDPI AG
2022-07-01
|
| Series: | International Journal of Molecular Sciences |
| Subjects: | |
| Online Access: | https://www.mdpi.com/1422-0067/23/14/7997 |
| _version_ | 1797433467087093760 |
|---|---|
| author | Maria E. Velizhanina Alexey P. Galkin |
| author_facet | Maria E. Velizhanina Alexey P. Galkin |
| author_sort | Maria E. Velizhanina |
| collection | DOAJ |
| description | Functional amyloids are fibrillary proteins with a cross-β structure that play a structural or regulatory role in pro- and eukaryotes. Previously, we have demonstrated that the RNA-binding FXR1 protein functions in an amyloid form in the rat brain. This RNA-binding protein plays an important role in the regulation of long-term memory, emotions, and cancer. Here, we evaluate the amyloid properties of FXR1 in organisms representing various classes of vertebrates. We show the colocalization of FXR1 with amyloid-specific dyes in the neurons of amphibians, reptiles, and birds. Moreover, FXR1, as with other amyloids, forms detergent-resistant insoluble aggregates in all studied animals. The FXR1 protein isolated by immunoprecipitation from the brains of different vertebrate species forms fibrils, which show yellow-green birefringence after staining with Congo red. Our data indicate that in the evolution of vertebrates, FXR1 acquired amyloid properties at least 365 million years ago. Based on the obtained data, we discuss the possible role of FXR1 amyloid fibrils in the regulation of vital processes in the brain of vertebrates. |
| first_indexed | 2024-03-09T10:17:26Z |
| format | Article |
| id | doaj.art-84fb7729ea864ff0935095afa95a4156 |
| institution | Directory Open Access Journal |
| issn | 1661-6596 1422-0067 |
| language | English |
| last_indexed | 2024-03-09T10:17:26Z |
| publishDate | 2022-07-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | International Journal of Molecular Sciences |
| spelling | doaj.art-84fb7729ea864ff0935095afa95a41562023-12-01T22:16:29ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672022-07-012314799710.3390/ijms23147997Amyloid Properties of the FXR1 Protein Are Conserved in Evolution of VertebratesMaria E. Velizhanina0Alexey P. Galkin1Laboratory of Amyloid Biology, St. Petersburg State University, Universitetskaya Emb. 7/9, 199034 St. Petersburg, RussiaDepartment of Genetics and Biotechnology, St. Petersburg State University, Universitetskaya Emb. 7/9, 199034 St. Petersburg, RussiaFunctional amyloids are fibrillary proteins with a cross-β structure that play a structural or regulatory role in pro- and eukaryotes. Previously, we have demonstrated that the RNA-binding FXR1 protein functions in an amyloid form in the rat brain. This RNA-binding protein plays an important role in the regulation of long-term memory, emotions, and cancer. Here, we evaluate the amyloid properties of FXR1 in organisms representing various classes of vertebrates. We show the colocalization of FXR1 with amyloid-specific dyes in the neurons of amphibians, reptiles, and birds. Moreover, FXR1, as with other amyloids, forms detergent-resistant insoluble aggregates in all studied animals. The FXR1 protein isolated by immunoprecipitation from the brains of different vertebrate species forms fibrils, which show yellow-green birefringence after staining with Congo red. Our data indicate that in the evolution of vertebrates, FXR1 acquired amyloid properties at least 365 million years ago. Based on the obtained data, we discuss the possible role of FXR1 amyloid fibrils in the regulation of vital processes in the brain of vertebrates.https://www.mdpi.com/1422-0067/23/14/7997functional amyloidFXR1 proteinbrainevolutionvertebratesfish |
| spellingShingle | Maria E. Velizhanina Alexey P. Galkin Amyloid Properties of the FXR1 Protein Are Conserved in Evolution of Vertebrates International Journal of Molecular Sciences functional amyloid FXR1 protein brain evolution vertebrates fish |
| title | Amyloid Properties of the FXR1 Protein Are Conserved in Evolution of Vertebrates |
| title_full | Amyloid Properties of the FXR1 Protein Are Conserved in Evolution of Vertebrates |
| title_fullStr | Amyloid Properties of the FXR1 Protein Are Conserved in Evolution of Vertebrates |
| title_full_unstemmed | Amyloid Properties of the FXR1 Protein Are Conserved in Evolution of Vertebrates |
| title_short | Amyloid Properties of the FXR1 Protein Are Conserved in Evolution of Vertebrates |
| title_sort | amyloid properties of the fxr1 protein are conserved in evolution of vertebrates |
| topic | functional amyloid FXR1 protein brain evolution vertebrates fish |
| url | https://www.mdpi.com/1422-0067/23/14/7997 |
| work_keys_str_mv | AT mariaevelizhanina amyloidpropertiesofthefxr1proteinareconservedinevolutionofvertebrates AT alexeypgalkin amyloidpropertiesofthefxr1proteinareconservedinevolutionofvertebrates |