RNA promotes phase separation of glycolysis enzymes into yeast G bodies in hypoxia.
Elife, 2020/04/16;9
Fuller GG[1], Han T[2], Freeberg MA[1], Moresco JJ[3], Ghanbari Niaki A[4], Roach NP[1], Yates JR 3rd[3], Myong S[4], Kim JK[1]
Affiliations
PMID: 32298230
Impact factor: 8.713
Abstract
In hypoxic stress conditions, glycolysis enzymes assemble into singular cytoplasmic granules called glycolytic (G) bodies. G body formation in yeast correlates with increased glucose consumption and cell survival. However, the physical properties and organizing principles that define G body formation are unclear. We demonstrate that glycolysis enzymes are non-canonical RNA binding proteins, sharing many common mRNA substrates that are also integral constituents of G bodies. Targeting nonspecific endoribonucleases to G bodies reveals that RNA nucleates G body formation and maintains its structural integrity. Consistent with a phase separation mechanism of biogenesis, recruitment of glycolysis enzymes to G bodies relies on multivalent homotypic and heterotypic interactions. Furthermore, G bodies fuse in vivo and are largely insensitive to 1,6-hexanediol, consistent with a hydrogel-like composition. Taken together, our results elucidate the biophysical nature of G bodies and demonstrate that RNA nucleates phase separation of the glycolysis machinery in response to hypoxic stress.
Keywords: RNA; S. cerevisiae; cell biology; glycolysis; hypoxia; phase separation
MeSH terms
Cytoplasmic Granules; Endoribonucleases; Glycolysis; RNA, Fungal; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins
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