Functional characterization of the ATPase-like activity displayed by a catalytic amyloid

• Published in: Biochimica et biophysica acta. General subjects Vol. 1865; no. 1; p. 129729
• Main Authors: Castillo-Caceres, Claudio, Duran-Meza, Eva, Nova, Esteban, Araya-Secchi, Raul, Monasterio, Octavio, Diaz-Espinoza, Rodrigo
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.01.2021
• Subjects: Adenosine Triphosphatases - chemistry; Adenosine Triphosphatases - metabolism; adenosine triphosphate; Adenosine Triphosphate - metabolism; Amino Acid Sequence; Amyloid; Amyloid - chemistry; Amyloid - metabolism; Amyloid - ultrastructure; Aspartate; aspartic acid; ATP; biotechnology; Catalysis; catalytic activity; circular dichroism spectroscopy; enzymes; fluorescence; Hydrolysis; manganese; Models, Molecular; Peptide; Peptides - chemistry; Peptides - metabolism; polypeptides; ribonucleotides; Substrate Specificity; transmission electron microscopy; Hydrolysis; Mn2; UTP; ThT; GTP; dATP; Aspartate; Amyloid; Catalysis; Peptide; ATP; CTP

Amyloids are highly ordered polypeptide aggregates stabilized by a beta-sheet structural core. Though classically associated to pathology, reports on novel functional roles of these proteins have increasingly emerged in the past decade. Moreover, the recent discovery that amyloids formed with ration...