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Comment
. 2023 Apr 21;21(4):e3002077.
doi: 10.1371/journal.pbio.3002077. eCollection 2023 Apr.

The breaking of fungal spore dormancy: A coordinated transition

Sjoerd Johan Seekles  1
Affiliations
Comment

The breaking of fungal spore dormancy: A coordinated transition

Sjoerd Johan Seekles. PLoS Biol. .

Abstract

The transition from dormant spore to germling has been topic of study and debate. A recent discovery in PLOS Biology shows that chaperone Hsp42 plays a crucial role in resolubilizing the proteome during dormancy breaking, although a role of trehalose cannot be excluded.

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Conflict of interest statement

The authors have declared that no competing interests exist.

Figures

Fig 1
Fig 1. Protein resolubilization during germination is at least in part orchestrated by chaperone Hsp42.
A cartoon visualizing protein resolubilization and the function of chaperone Hsp42 during this transition. Metabolically (nearly) inactive fungal spores contain a highly viscous cytoplasm. The highly viscous cytoplasm resembles a “glassy state” in which proteins are preserved and inactive. During germination, the viscous cytoplasm transitions to a watery cytoplasm. Some proteins resolubilize earlier than others, one such protein is chaperone Hsp42. During early stages of germination, Hsp42 gets phosphorylated and, therefore, activated and ensures proper refolding and resolubilization of the spore’s proteome.
See this image and copyright information in PMC

Comment on

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