Light-dependent modulation of protein localization and function in living bacteria cells
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...
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| Format: | Article |
| Language: | English |
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Nature Portfolio
2024-12-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-024-54974-9 |
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| author | 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 Malcolm E. Winkler Erin D. Goley Kumaran S. Ramamurthi Jie Xiao |
| author_facet | 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 Malcolm E. Winkler Erin D. Goley Kumaran S. Ramamurthi Jie Xiao |
| author_sort | Ryan McQuillen |
| collection | DOAJ |
| description | 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. |
| format | Article |
| id | doaj-art-f2380f756e734a39bc8b2a4768ba67c8 |
| institution | Kabale University |
| issn | 2041-1723 |
| language | English |
| publishDate | 2024-12-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Nature Communications |
| spelling | doaj-art-f2380f756e734a39bc8b2a4768ba67c82025-01-05T12:35:54ZengNature PortfolioNature Communications2041-17232024-12-0115111510.1038/s41467-024-54974-9Light-dependent modulation of protein localization and function in living bacteria cellsRyan McQuillen0Amilcar J. Perez1Xinxing Yang2Christopher H. Bohrer3Erika L. Smith4Sylvia Chareyre5Ho-Ching Tiffany Tsui6Kevin E. Bruce7Yin Mon Hla8Joshua W. McCausland9Malcolm E. Winkler10Erin D. Goley11Kumaran S. Ramamurthi12Jie Xiao13Department of Biophysics & Biophysical Chemistry, The Johns Hopkins University School of MedicineDepartment of Biophysics & Biophysical Chemistry, The Johns Hopkins University School of MedicineDepartment of Biophysics & Biophysical Chemistry, The Johns Hopkins University School of MedicineDepartment of Biophysics & Biophysical Chemistry, The Johns Hopkins University School of MedicineDepartment of Biological Chemistry, The Johns Hopkins University School of MedicineLaboratory of Molecular Biology, National Cancer Institute, National Institutes of HealthDepartment of Biology, Indiana University BloomingtonDepartment of Biology, Indiana University BloomingtonDepartment of Biology, Indiana University BloomingtonDepartment of Biophysics & Biophysical Chemistry, The Johns Hopkins University School of MedicineDepartment of Biology, Indiana University BloomingtonDepartment of Biological Chemistry, The Johns Hopkins University School of MedicineLaboratory of Molecular Biology, National Cancer Institute, National Institutes of HealthDepartment of Biophysics & Biophysical Chemistry, The Johns Hopkins University School of MedicineAbstract 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.https://doi.org/10.1038/s41467-024-54974-9 |
| spellingShingle | 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 Malcolm E. Winkler Erin D. Goley Kumaran S. Ramamurthi Jie Xiao Light-dependent modulation of protein localization and function in living bacteria cells Nature Communications |
| title | Light-dependent modulation of protein localization and function in living bacteria cells |
| title_full | Light-dependent modulation of protein localization and function in living bacteria cells |
| title_fullStr | Light-dependent modulation of protein localization and function in living bacteria cells |
| title_full_unstemmed | Light-dependent modulation of protein localization and function in living bacteria cells |
| title_short | Light-dependent modulation of protein localization and function in living bacteria cells |
| title_sort | light dependent modulation of protein localization and function in living bacteria cells |
| url | https://doi.org/10.1038/s41467-024-54974-9 |
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