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Amyloid Properties of the FXR1 Protein Are Conserved in Evolution of Vertebrates. / Velizhanina, Maria E.; Galkin, Alexey P.
In: International Journal of Molecular Sciences, Vol. 23, No. 14, 7997, 20.07.2022.Research output: Contribution to journal › Article › peer-review
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TY - JOUR
T1 - Amyloid Properties of the FXR1 Protein Are Conserved in Evolution of Vertebrates
AU - Velizhanina, Maria E.
AU - Galkin, Alexey P.
PY - 2022/7/20
Y1 - 2022/7/20
N2 - 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.
AB - 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.
KW - amphibians
KW - birds
KW - brain
KW - evolution
KW - fish
KW - functional amyloid
KW - FXR1 protein
KW - mammals
KW - reptiles
KW - vertebrates
UR - http://www.scopus.com/inward/record.url?scp=85135126792&partnerID=8YFLogxK
U2 - 10.3390/ijms23147997
DO - 10.3390/ijms23147997
M3 - Article
C2 - 35887344
AN - SCOPUS:85135126792
VL - 23
JO - International Journal of Molecular Sciences
JF - International Journal of Molecular Sciences
SN - 1422-0067
IS - 14
M1 - 7997
ER -
ID: 102041083