Dissecting the molecular properties of prokaryotic flotillins.
Flotillins are universally conserved proteins that are present in all kingdoms of life. Recently it was demonstrated that the B. subtilis flotillin YuaG (FloT) has a direct influence on membrane domain formation by orchestrating lipid domains. Thereby it allocates a proper environment for diverse ce...
| প্রধান লেখক: | , |
|---|---|
| বিন্যাস: | প্রবন্ধ |
| ভাষা: | English |
| প্রকাশিত: |
Public Library of Science (PLoS)
2015-01-01
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| মালা: | PLoS ONE |
| অনলাইন ব্যবহার করুন: | http://europepmc.org/articles/PMC4312047?pdf=render |
| _version_ | 1828794028877938688 |
|---|---|
| author | Juri Niño Bach Marc Bramkamp |
| author_facet | Juri Niño Bach Marc Bramkamp |
| author_sort | Juri Niño Bach |
| collection | DOAJ |
| description | Flotillins are universally conserved proteins that are present in all kingdoms of life. Recently it was demonstrated that the B. subtilis flotillin YuaG (FloT) has a direct influence on membrane domain formation by orchestrating lipid domains. Thereby it allocates a proper environment for diverse cellular machineries. YuaG creates platforms for signal transduction, processes crucial for biofilm formation, sporulation, competence, secretion, and others. Even though, flotillins are an emerging topic of research in the field of microbiology little is known about the molecular architecture of prokaryotic flotillins. All flotillins share common structural elements and are tethered to the membrane N'- terminally, followed by a so called PHB domain and a flotillin domain. We show here that prokaryotic flotillins are, similarly to eukaryotic flotillins, tethered to the membrane via a hairpin loop. Further it is demonstrated by sedimentation assays that B. subtilis flotillins do not bind to the membrane via their PHB domain contrary to eukaryotic flotillins. Size exclusion chromatography experiments, blue native PAGE and cross linking experiments revealed that B. subtilis YuaG can oligomerize into large clusters via the PHB domain. This illustrates an important difference in the setup of prokaryotic flotillins compared to the organization of eukaryotic flotillins. |
| first_indexed | 2024-12-12T03:36:52Z |
| format | Article |
| id | doaj.art-6a7b938b4ab14b5baf7d1c61e8a0dd8a |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-12-12T03:36:52Z |
| publishDate | 2015-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj.art-6a7b938b4ab14b5baf7d1c61e8a0dd8a2022-12-22T00:39:46ZengPublic Library of Science (PLoS)PLoS ONE1932-62032015-01-01101e011675010.1371/journal.pone.0116750Dissecting the molecular properties of prokaryotic flotillins.Juri Niño BachMarc BramkampFlotillins are universally conserved proteins that are present in all kingdoms of life. Recently it was demonstrated that the B. subtilis flotillin YuaG (FloT) has a direct influence on membrane domain formation by orchestrating lipid domains. Thereby it allocates a proper environment for diverse cellular machineries. YuaG creates platforms for signal transduction, processes crucial for biofilm formation, sporulation, competence, secretion, and others. Even though, flotillins are an emerging topic of research in the field of microbiology little is known about the molecular architecture of prokaryotic flotillins. All flotillins share common structural elements and are tethered to the membrane N'- terminally, followed by a so called PHB domain and a flotillin domain. We show here that prokaryotic flotillins are, similarly to eukaryotic flotillins, tethered to the membrane via a hairpin loop. Further it is demonstrated by sedimentation assays that B. subtilis flotillins do not bind to the membrane via their PHB domain contrary to eukaryotic flotillins. Size exclusion chromatography experiments, blue native PAGE and cross linking experiments revealed that B. subtilis YuaG can oligomerize into large clusters via the PHB domain. This illustrates an important difference in the setup of prokaryotic flotillins compared to the organization of eukaryotic flotillins.http://europepmc.org/articles/PMC4312047?pdf=render |
| spellingShingle | Juri Niño Bach Marc Bramkamp Dissecting the molecular properties of prokaryotic flotillins. PLoS ONE |
| title | Dissecting the molecular properties of prokaryotic flotillins. |
| title_full | Dissecting the molecular properties of prokaryotic flotillins. |
| title_fullStr | Dissecting the molecular properties of prokaryotic flotillins. |
| title_full_unstemmed | Dissecting the molecular properties of prokaryotic flotillins. |
| title_short | Dissecting the molecular properties of prokaryotic flotillins. |
| title_sort | dissecting the molecular properties of prokaryotic flotillins |
| url | http://europepmc.org/articles/PMC4312047?pdf=render |
| work_keys_str_mv | AT jurininobach dissectingthemolecularpropertiesofprokaryoticflotillins AT marcbramkamp dissectingthemolecularpropertiesofprokaryoticflotillins |