Evidence map›Paper›PMID 32814039›Full record

ArticleCell reports2020

Daily Cycles of Reversible Protein Condensation in Cyanobacteria.

Gopal K Pattanayak, Yi Liao, Edward W J Wallace, Bogdan Budnik, D Allan Drummond, Michael J Rust

Open access · goldAbstract read
In one paragraph

Article in Cell reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed, 1 pooled it
2.9field-weighted citation impact, top 8% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

20 citing papers in PubMed, 1 synthesis or guideline pooled it, 38 citations in OpenAlex.

  1. Pooled it
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  15. Article
  16. Protein conformation and biomolecular condensates.Current research in structural biology · 2022
    Review
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  18. Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 1 country.

Gopal K PattanayakDepartment of Molecular Genetics and Cell Biology, University of Chicago, Chicago, IL 60637, USA.
Yi LiaoDepartment of Molecular Genetics and Cell Biology, University of Chicago, Chicago, IL 60637, USA.
Edward W J WallaceDepartment of Biochemistry and Molecular Biology, University of Chicago, Chicago, IL 60637, USA.
Bogdan BudnikMass Spectrometry and Proteomics Resource Laboratory, FAS Division of Science, Harvard University, Cambridge, MA 02138, USA.
D Allan DrummondDepartment of Biochemistry and Molecular Biology, University of Chicago, Chicago, IL 60637, USA.
Michael J RustDepartment of Molecular Genetics and Cell Biology, University of Chicago, Chicago, IL 60637, USA; Department of Physics, University of Chicago, Chicago, IL 60637, USA. Electronic address: mrust@uchicago.edu.
University of Chicago · USHarvard University · US

Funding

Determining the molecular basis of adaptive stress-triggered protein phase separationR01GM126547 · NIGMS · UNIVERSITY OF CHICAGO · PI DRUMMOND, DAVID ALLAN, SOSNICK, TOBIN R · 2018 to 2021
$1.6M
Coupling between Circadian Rhythms and Metaboilsm in CyanobacteriaR01GM107369 · NIGMS · UNIVERSITY OF CHICAGO · PI RUST, MICHAEL · 2013 to 2017
$1.5M
The Biochemistry of Clock Function in Fluctuating EnvironmentsR01GM135382 · NIGMS · UNIVERSITY OF CHICAGO · PI RUST, MICHAEL · 2020 to 2023
$1.3M
Signatures of interaction-driven selection on low-complexity sequencesR01GM127406 · NIGMS · UNIVERSITY OF CHICAGO · PI DRUMMOND, DAVID ALLAN · 2018 to 2021
$1.1M
Howard Hughes Medical InstituteNIGMS NIH HHS R01 GM107369NIGMS NIH HHS R01 GM126547NIGMS NIH HHS R01 GM127406NIGMS NIH HHS R01 GM135382
6 · The paper itself

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.

Indexed as

CyanobacteriaProtein Conformationcircadian clockcyanobacteriametabolismprotein condensation

Identifiers

PMID32814039
PMCPMC10005845
OpenAlexW3057324553

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.