Evidence map›Paper›PMID 39737933›Full record

ArticleNature communications2024

Light-dependent modulation of protein localization and function in living bacteria cells.

Ryan McQuillen, Amilcar J Perez, Xinxing Yang, Christopher H Bohrer, Erika L Smith, Sylvia Chareyre, Ho-Ching Tiffany Tsui, Kevin E Bruce, Yin Mon Hla, Joshua W McCausland and 4 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
–field-weighted citation impact
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

6 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Direct Quantification of Protein-Protein Interactions in Living Bacterial Cells.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article
  6. Review
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

14 authors.

Ryan McQuillen *Department of Biophysics & Biophysical Chemistry, The Johns Hopkins University School of Medicine, Baltimore, MD, USA.ORCID 0000-0002-0399-5248
Amilcar J Perez *Department of Biophysics & Biophysical Chemistry, The Johns Hopkins University School of Medicine, Baltimore, MD, USA.
Xinxing YangDepartment of Biophysics & Biophysical Chemistry, The Johns Hopkins University School of Medicine, Baltimore, MD, USA.ORCID 0000-0002-2101-9881
Christopher H BohrerDepartment of Biophysics & Biophysical Chemistry, The Johns Hopkins University School of Medicine, Baltimore, MD, USA.
Erika L SmithDepartment of Biological Chemistry, The Johns Hopkins University School of Medicine, Baltimore, MD, USA.ORCID 0000-0003-2665-3408
Sylvia ChareyreLaboratory of Molecular Biology, National Cancer Institute, National Institutes of Health, Bethesda, MD, USA.
Ho-Ching Tiffany TsuiDepartment of Biology, Indiana University Bloomington, Bloomington, IN, USA.ORCID 0000-0003-0849-874X
Kevin E BruceDepartment of Biology, Indiana University Bloomington, Bloomington, IN, USA.ORCID 0009-0005-3300-8863
Yin Mon HlaDepartment of Biology, Indiana University Bloomington, Bloomington, IN, USA.
Joshua W McCauslandDepartment of Biophysics & Biophysical Chemistry, The Johns Hopkins University School of Medicine, Baltimore, MD, USA.ORCID 0000-0001-6585-0506
Malcolm E WinklerDepartment of Biology, Indiana University Bloomington, Bloomington, IN, USA.ORCID 0000-0002-1482-2588
Erin D GoleyDepartment of Biological Chemistry, The Johns Hopkins University School of Medicine, Baltimore, MD, USA.ORCID 0000-0002-8518-2303
Kumaran S RamamurthiLaboratory of Molecular Biology, National Cancer Institute, National Institutes of Health, Bethesda, MD, USA.ORCID 0000-0002-2335-3568
Jie XiaoDepartment of Biophysics & Biophysical Chemistry, The Johns Hopkins University School of Medicine, Baltimore, MD, USA. xiao@jhmi.edu.ORCID 0000-0003-1433-5437

Funding

PROGRAM IN MOLECULAR BIOPHYSICST32GM008403 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI BARRICK, DOUGLAS E. · 1990 to 2019
$13.5M
Biochemistry, Cellular and Molecular Biology Program: JHU BioGREAT (Biomedical Graduate REsiliency & Adaptability Training)T32GM144272 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI Takanari Inoue · 2022 to 2026
$5.4M
Program of Molecular BiophysicsT32GM135131 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI Karen G. Fleming · 2020 to 2026
$5.4M
New Regulatory Interactions and Circuits that Mediate the Dynamics, Homeostasis, and Stress Responses of Peptidoglycan Synthesis in the Superbug Streptococcus pneumoniaeR35GM131767 · NIGMS · TRUSTEES OF INDIANA UNIVERSITY · PI MALCOLM E. WINKLER · 2019 to 2026
$4.8M
Spatial Organization and Regulation of Bacterial Cellular ProcessesR35GM136436 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI Jie Xiao · 2020 to 2026
$4.8M
Probing the structure, dynamics and function of the E. coli divisomeR01GM086447 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI XIAO, JIE · 2011 to 2019
$3.8M
Local and global regulation of bacterial growthR35GM136221 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI Erin D Goley · 2020 to 2026
$3.0M
Elucidating the spatiotemporal regulation of septal peptidoglycan synthases in E.coliF32GM150262 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI PEREZ, AMILCAR JOSUE · 2023 to 2024
$151k
NIGMS NIH HHS F32 GM150262NIGMS NIH HHS R01 GM086447NIGMS NIH HHS R35 GM131767NIGMS NIH HHS R35 GM136221NIGMS NIH HHS R35 GM136436NIGMS NIH HHS T32 GM008403NIGMS NIH HHS T32 GM135131NIGMS NIH HHS T32 GM144272U.S. Department of Health & Human Services | NIH | National Institute of General Medical Sciences (NIGMS) GM008403U.S. Department of Health & Human Services | NIH | National Institute of General Medical Sciences (NIGMS) GM131767U.S. Department of Health & Human Services | NIH | National Institute of General Medical Sciences (NIGMS) GM136221U.S. Department of Health & Human Services | NIH | National Institute of General Medical Sciences (NIGMS) GM136436U.S. Department of Health & Human Services | NIH | National Institute of General Medical Sciences (NIGMS) GM144272U.S. Department of Health & Human Services | NIH | National Institute of General Medical Sciences (NIGMS) GM150262
6 · The paper itself

Abstract

Most bacteria lack membrane-enclosed organelles and rely on macromolecular scaffolds at different subcellular locations to recruit proteins for specific functions. Here, we demonstrate that the optogenetic CRY2-CIB1 system from Arabidopsis thaliana can be used to rapidly direct proteins to different subcellular locations with varying efficiencies in live Escherichia coli cells, including the nucleoid, the cell pole, the membrane, and the midcell division plane. Such light-induced re-localization can be used to rapidly inhibit cytokinesis in actively dividing E. coli cells. We further show that CRY2-CIBN binding kinetics can be modulated by green light, adding a new dimension of control to the system. Finally, we test this optogenetic system in three additional bacterial species, Bacillus subtilis, Caulobacter crescentus, and Streptococcus pneumoniae, providing important considerations for this system's applicability in bacterial cell biology.

Indexed as

ArabidopsisArabidopsis ProteinsBacillus subtilisCaulobacter crescentusEscherichia coliLightOptogeneticsBacterial ProteinsCryptochromesCytokinesisProtein TransportStreptococcus pneumoniaeArabidopsis ProteinsBacterial ProteinsCRY2 protein, ArabidopsisCryptochromes

Identifiers

PMID39737933
PMCPMC11685620

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.