Identification of New FG-Repeat Nucleoporins with Amyloid Properties

Amyloids are fibrillar protein aggregates with a cross-β structure. More than two hundred different proteins with amyloid or amyloid-like properties are already known. Functional amyloids with conservative amyloidogenic regions were found in different organisms. Protein aggregation appears to be ben...

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Bibliographic Details
Published in:	International journal of molecular sciences Vol. 24; no. 10; p. 8571
Main Authors:	Danilov, Lavrentii G, Sukhanova, Xenia V, Rogoza, Tatiana M, Antonova, Ekaterina Y, Trubitsina, Nina P, Zhouravleva, Galina A, Bondarev, Stanislav A
Format:	Journal Article
Language:	English
Published:	Switzerland MDPI AG 10-05-2023 MDPI
Subjects:	Aggregates Alzheimer's disease Amino acids Amyloid - metabolism Amyloidogenesis Amyloidogenic Proteins - metabolism amyloids Analysis Animals ArchCandy Bacteria C-DAG Conservatism CPEB protein Drosophila melanogaster Drosophila melanogaster - genetics Drosophila melanogaster - metabolism evolution FG-repeats Fibrils Fruit flies FXR1 protein Glycine Glycoproteins Humans Hydrogels Long term memory Mice Nuclear Pore Complex Proteins - metabolism Nuclear Proteins - metabolism Nucleoporins Phenylalanine Plasmids Protein interaction Proteins RNA-Binding Proteins - metabolism Saccharomyces cerevisiae - genetics Saccharomyces cerevisiae - metabolism Saccharomyces cerevisiae Proteins - metabolism Signal transduction Type 2 diabetes Vertebrates Yeast Russia amyloids FG-repeats ArchCandy evolution C-DAG nucleoporins
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Summary:	Amyloids are fibrillar protein aggregates with a cross-β structure. More than two hundred different proteins with amyloid or amyloid-like properties are already known. Functional amyloids with conservative amyloidogenic regions were found in different organisms. Protein aggregation appears to be beneficial for the organism in these cases. Therefore, this property might be conservative for orthologous proteins. The amyloid aggregates of the CPEB protein were suggested to play an important role in the long-term memory formation in , , and . Moreover, the FXR1 protein demonstrates amyloid properties among the Vertebrates. A few nucleoporins (e.g., yeast Nup49, Nup100, Nup116, and human Nup153 and Nup58), are supposed or proved to form amyloid fibrils. In this study, we performed wide-scale bioinformatic analysis of nucleoporins with FG-repeats (phenylalanine-glycine repeats). We demonstrated that most of the barrier nucleoporins possess potential amyloidogenic properties. Furthermore, the aggregation-prone properties of several Nsp1 and Nup100 orthologs in bacteria and yeast cells were analyzed. Only two new nucleoporins, Nup98 and Nup98, aggregated in different experiments. At the same time, Nup58 only formed amyloids in bacterial cells. These results rather contradict the hypothesis about the functional aggregation of nucleoporins.
Bibliography:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	1422-0067 1661-6596 1422-0067
DOI:	10.3390/ijms24108571