N-terminal region of Drosophila melanogaster Argonaute2 forms amyloid-like aggregates

• Published in: BMC biology Vol. 21; no. 1; pp. 78 - 12
• Main Authors: Narita, Haruka, Shima, Tomohiro, Iizuka, Ryo, Uemura, Sotaro
• Format: Journal Article
• Language: English
• Published: England BioMed Central Ltd 19.04.2023; BioMed Central; BMC
• Subjects: Agglomeration; Aggregates; Aggregation; Algorithms; Amino acids; Amyloid; Amyloid - metabolism; Animals; Argonaute; Argonaute Proteins - genetics; Argonaute Proteins - metabolism; Composition; Drosophila; Drosophila melanogaster; Drosophila melanogaster - metabolism; Fluorescence; Fluorescence microscopy; Fractals; Fruit flies; Gene silencing; Genetic aspects; Glutamine; Glycine; Identification and classification; In vivo methods and tests; Insects; Methods; Microscopy; Peptides; Peptides - metabolism; Prion; Prions - chemistry; Protein Aggregates; Proteins; Reagents; RNA; RNA interference; RNA-mediated interference; Self propagation; Sodium dodecyl sulfate; Sodium lauryl sulfate; Sulfates; Surface active agents; Testing; Japan; Aggregation; Amyloid; Prion; RNA interference; Argonaute

Argonaute proteins play a central role in RNA silencing by forming protein-small RNA complexes responsible for the silencing process. While most Argonaute proteins have a short N-terminal region, Argonaute2 in Drosophila melanogaster (DmAgo2) harbors a long and unique N-terminal region. Previous in...