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CryoEM reveals that ribosomes in microsporidian spores are locked in a dimeric hibernating state

ABSTRACT: Translational control is an essential process for the cell to adapt to varying physiological or environmental conditions. To survive adverse conditions such as low nutrient levels, translation can be shut down almost entirely by inhibiting ribosomal function. Here we investigated eukaryotic hibernating ribosomes from the microsporidian parasite Spraguea lophii in situ by a combination of electron cryo-tomography (cryoET) and single particle cryoEM. We show that microsporidian spores contain hibernating ribosomes that are locked in the 100 S dimeric state, which is formed by a unique dimerisation mechanism involving the beak region. The ribosomes within the dimer are fully assembled, suggesting that they are ready to be activated once the host cell is invaded. This study provides structural evidence for dimerisation acting as a mechanism for ribosomal hibernation in microsporidia, and therefore demonstrates that eukaryotes utilise this mechanism in translational control.

INSTRUMENT(S):

ORGANISM(S): Spraguea Lophii 42_110

TISSUE(S): Fungal Spore

DISEASE(S): Microsporidiosis

SUBMITTER: Rebecca Conners

LAB HEAD: Bertram Daum

PROVIDER: PXD044467 | Pride | 2025-12-01

REPOSITORIES: Pride

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			Action	DRS
	281020_Sample_1.raw	Raw
	281020_Sample_1_PS.msf	Msf
	281020_Sample_2.raw	Raw
	281020_Sample_2_PS.msf	Msf
	281020_Sample_3.raw	Raw

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