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.
journal_name
Elifejournal_title
eLifeauthors
Fuller GG,Han T,Freeberg MA,Moresco JJ,Ghanbari Niaki A,Roach NP,Yates JR 3rd,Myong S,Kim JKdoi
10.7554/eLife.48480subject
Has Abstractpub_date
2020-04-16 00:00:00issn
2050-084Xpii
48480journal_volume
9pub_type
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