Cellular uptake of nickel by NikR is regulated by phase separation
Summary: Bacterial cells were long thought to be “bags of enzymes” with minimal internal structures. In recent years, membrane-less organelles formed by liquid-liquid phase separation (LLPS) of proteins or nucleic acids have been found to be involved in many important biological processes, although...
| Main Authors: | , , , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Elsevier
2023-06-01
|
| Series: | Cell Reports |
| Subjects: | |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S2211124723005296 |
| _version_ | 1797822558491377664 |
|---|---|
| author | Kaiming Cao Shixuan Li Yu Wang Hongze Hu Sijia Xiang Qianling Zhang Yangzhong Liu |
| author_facet | Kaiming Cao Shixuan Li Yu Wang Hongze Hu Sijia Xiang Qianling Zhang Yangzhong Liu |
| author_sort | Kaiming Cao |
| collection | DOAJ |
| description | Summary: Bacterial cells were long thought to be “bags of enzymes” with minimal internal structures. In recent years, membrane-less organelles formed by liquid-liquid phase separation (LLPS) of proteins or nucleic acids have been found to be involved in many important biological processes, although most of them were studied on eukaryotic cells. Here, we report that NikR, a bacterial nickel-responsive regulatory protein, exhibits LLPS both in solution and inside cells. Analyses of cellular nickel uptake and cell growth of E. coli confirm that LLPS enhances the regulatory function of NikR, while disruption of LLPS in cells promotes the expression of nickel transporter (nik) genes, which are negatively regulated by NikR. Mechanistic study shows that Ni(II) ions induces the accumulation of nik promoter DNA into the condensates formed by NikR. This result suggests that the formation of membrane-less compartments can be a regulatory mechanism of metal transporter proteins in bacterial cells. |
| first_indexed | 2024-03-13T10:10:52Z |
| format | Article |
| id | doaj.art-c61a930ea28d4285a5e52af1354a11f4 |
| institution | Directory Open Access Journal |
| issn | 2211-1247 |
| language | English |
| last_indexed | 2024-03-13T10:10:52Z |
| publishDate | 2023-06-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Cell Reports |
| spelling | doaj.art-c61a930ea28d4285a5e52af1354a11f42023-05-22T04:04:48ZengElsevierCell Reports2211-12472023-06-01426112518Cellular uptake of nickel by NikR is regulated by phase separationKaiming Cao0Shixuan Li1Yu Wang2Hongze Hu3Sijia Xiang4Qianling Zhang5Yangzhong Liu6College of Chemistry and Environmental Engineering, College of Physics and Optoelectronic Engineering, Shenzhen University, Shenzhen 518060, China; Department of Chemistry, University of Science and Technology of China, Hefei 230026, ChinaDepartment of Chemistry, University of Science and Technology of China, Hefei 230026, ChinaDepartment of Chemistry, University of Science and Technology of China, Hefei 230026, ChinaDepartment of Chemistry, University of Science and Technology of China, Hefei 230026, ChinaDepartment of Chemistry, University of Science and Technology of China, Hefei 230026, ChinaCollege of Chemistry and Environmental Engineering, College of Physics and Optoelectronic Engineering, Shenzhen University, Shenzhen 518060, China; Corresponding authorDepartment of Chemistry, University of Science and Technology of China, Hefei 230026, China; Corresponding authorSummary: Bacterial cells were long thought to be “bags of enzymes” with minimal internal structures. In recent years, membrane-less organelles formed by liquid-liquid phase separation (LLPS) of proteins or nucleic acids have been found to be involved in many important biological processes, although most of them were studied on eukaryotic cells. Here, we report that NikR, a bacterial nickel-responsive regulatory protein, exhibits LLPS both in solution and inside cells. Analyses of cellular nickel uptake and cell growth of E. coli confirm that LLPS enhances the regulatory function of NikR, while disruption of LLPS in cells promotes the expression of nickel transporter (nik) genes, which are negatively regulated by NikR. Mechanistic study shows that Ni(II) ions induces the accumulation of nik promoter DNA into the condensates formed by NikR. This result suggests that the formation of membrane-less compartments can be a regulatory mechanism of metal transporter proteins in bacterial cells.http://www.sciencedirect.com/science/article/pii/S2211124723005296CP: Molecular biologyCP: Cell biology |
| spellingShingle | Kaiming Cao Shixuan Li Yu Wang Hongze Hu Sijia Xiang Qianling Zhang Yangzhong Liu Cellular uptake of nickel by NikR is regulated by phase separation Cell Reports CP: Molecular biology CP: Cell biology |
| title | Cellular uptake of nickel by NikR is regulated by phase separation |
| title_full | Cellular uptake of nickel by NikR is regulated by phase separation |
| title_fullStr | Cellular uptake of nickel by NikR is regulated by phase separation |
| title_full_unstemmed | Cellular uptake of nickel by NikR is regulated by phase separation |
| title_short | Cellular uptake of nickel by NikR is regulated by phase separation |
| title_sort | cellular uptake of nickel by nikr is regulated by phase separation |
| topic | CP: Molecular biology CP: Cell biology |
| url | http://www.sciencedirect.com/science/article/pii/S2211124723005296 |
| work_keys_str_mv | AT kaimingcao cellularuptakeofnickelbynikrisregulatedbyphaseseparation AT shixuanli cellularuptakeofnickelbynikrisregulatedbyphaseseparation AT yuwang cellularuptakeofnickelbynikrisregulatedbyphaseseparation AT hongzehu cellularuptakeofnickelbynikrisregulatedbyphaseseparation AT sijiaxiang cellularuptakeofnickelbynikrisregulatedbyphaseseparation AT qianlingzhang cellularuptakeofnickelbynikrisregulatedbyphaseseparation AT yangzhongliu cellularuptakeofnickelbynikrisregulatedbyphaseseparation |