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Daily Cycles of Reversible Protein Condensation in Cyanobacteria.


ABSTRACT: An emerging principle of cell biology is the regulated conversion of macromolecules between soluble and condensed states. To screen for such regulation of the cyanobacterial proteome, we use quantitative mass spectrometry to identify proteins that change solubility during the day-night cycle. We find a set of night-insoluble proteins that includes many enzymes in essential metabolic pathways. Using time-lapse microscopy and isotope labeling, we show that these proteins reversibly transition between punctate structures at night and a soluble state during the day without substantial degradation. We find that the cyanobacterial circadian clock regulates the kinetics of puncta formation during the night and that the appearance of puncta indicates the metabolic status of the cell. Reversible condensation of specific enzymes is thus a regulated response to the day-night cycle and may reflect a general bacterial strategy used in fluctuating growth conditions.

SUBMITTER: Pattanayak GK 

PROVIDER: S-EPMC10005845 | biostudies-literature | 2020 Aug

REPOSITORIES: biostudies-literature

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Daily Cycles of Reversible Protein Condensation in Cyanobacteria.

Pattanayak Gopal K GK   Liao Yi Y   Wallace Edward W J EWJ   Budnik Bogdan B   Drummond D Allan DA   Rust Michael J MJ  

Cell reports 20200801 7


An emerging principle of cell biology is the regulated conversion of macromolecules between soluble and condensed states. To screen for such regulation of the cyanobacterial proteome, we use quantitative mass spectrometry to identify proteins that change solubility during the day-night cycle. We find a set of night-insoluble proteins that includes many enzymes in essential metabolic pathways. Using time-lapse microscopy and isotope labeling, we show that these proteins reversibly transition betw  ...[more]

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