Premium
Amyloid‐mediated translational control is required for meiosis
Author(s) -
Berchowitz Luke E.,
Walker Margaret R.,
Kabachinski Gregory L.,
Schwartz Thomas U.,
Amon Angelika
Publication year - 2017
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.31.1_supplement.525.4
Subject(s) - meiosis , translation (biology) , microbiology and biotechnology , amyloid (mycology) , biology , chromosome segregation , translational regulation , protein aggregation , gametogenesis , psychological repression , genetics , messenger rna , gene expression , gene , chromosome , embryo , botany , cryopreservation
Amyloids are fibrous protein aggregates that are associated with, and often causative of, numerous human diseases including Alzheimer's, Parkinson's, and diabetes. Amyloids are thought to trigger disease by forming insoluble aggregates composed of inactive protein that interfere with cell viability. Whether and how amyloid properties of proteins participate in cellular functions is poorly understood. We uncoverd a physiological role for amyloids in the regulation of mRNA translation. In budding yeast, repression of translation of the B‐type cyclin CLB3 during meiosis I is essential for establishing the unique meiotic chromosome segregation pattern and for gametogenesis. The meiosis‐specific RNA‐binding protein Rim4 mediates this translational repression. We find that Rim4 forms amyloids, fibrous protein aggregates, and that it is amyloid form of Rim4 that is the active, translationally repressive form of the protein. Our data further show that amyloid formation is a developmentally regulated process. Starvation, one of the signals that triggers gamete development, induces the conversion of monomeric Rim4 into amyloid thereby activating the protein to bring about repression of CLB3 translation. At the onset of meiosis II, Rim4 amyloids are abruptly degraded allowing CLB3 translation to commence. We conclude that proteins can utilize their amyloid‐forming properties to function as central regulators of gametogenesis. Support or Funding Information HHMI & NIH