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| | ==Solution structure of the B. subtilis anti-sigma-F factor, FIN== | | ==Solution structure of the B. subtilis anti-sigma-F factor, FIN== |
| - | <StructureSection load='5msl' size='340' side='right'caption='[[5msl]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='5msl' size='340' side='right'caption='[[5msl]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5msl]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MSL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5MSL FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5msl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MSL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5MSL FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fin, subA, yabK, BSU00540 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 "Vibrio subtilis" Ehrenberg 1835])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5msl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5msl OCA], [http://pdbe.org/5msl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5msl RCSB], [http://www.ebi.ac.uk/pdbsum/5msl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5msl ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5msl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5msl OCA], [https://pdbe.org/5msl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5msl RCSB], [https://www.ebi.ac.uk/pdbsum/5msl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5msl ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/FIN_BACSU FIN_BACSU]] An anti-sigma factor for sporulation specific sigma-F factor, by antagonizing sigma-F it allows the switch to sigma-G factor and progression to the late sporulation development stages (PubMed:21037003). Might stabilize or process Holliday junction intermediates, although this may be due to polar effects on the downstream mfd gene (PubMed:15317759).<ref>PMID:15317759</ref> <ref>PMID:21037003</ref> | + | [https://www.uniprot.org/uniprot/FIN_BACSU FIN_BACSU] An anti-sigma factor for sporulation specific sigma-F factor, by antagonizing sigma-F it allows the switch to sigma-G factor and progression to the late sporulation development stages (PubMed:21037003). Might stabilize or process Holliday junction intermediates, although this may be due to polar effects on the downstream mfd gene (PubMed:15317759).<ref>PMID:15317759</ref> <ref>PMID:21037003</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Vibrio subtilis ehrenberg 1835]] | + | [[Category: Bacillus subtilis]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Alfano, C]] | + | [[Category: Alfano C]] |
| - | [[Category: Isaacson, R L]] | + | [[Category: Isaacson RL]] |
| - | [[Category: Martinez-Lumbreras, S]] | + | [[Category: Martinez-Lumbreras S]] |
| - | [[Category: Bacillus subtili]]
| + | |
| - | [[Category: Sigma factor]]
| + | |
| - | [[Category: Sporulation]]
| + | |
| - | [[Category: Transcription]]
| + | |
| - | [[Category: Zinc finger]]
| + | |
| Structural highlights
Function
FIN_BACSU An anti-sigma factor for sporulation specific sigma-F factor, by antagonizing sigma-F it allows the switch to sigma-G factor and progression to the late sporulation development stages (PubMed:21037003). Might stabilize or process Holliday junction intermediates, although this may be due to polar effects on the downstream mfd gene (PubMed:15317759).[1] [2]
Publication Abstract from PubMed
Sporulation in Bacillus subtilis is governed by a cascade of alternative RNA polymerase sigma factors. We previously identified a small protein Fin that is produced under the control of the sporulation sigma factor sigmaF to create a negative feedback loop that inhibits sigmaF -directed gene transcription. Cells deleted for fin are defective for spore formation and exhibit increased levels of sigmaF -directed gene transcription. Based on pull-down experiments, chemical crosslinking, bacterial two-hybrid experiments and nuclear magnetic resonance chemical shift analysis, we now report that Fin binds to RNA polymerase and specifically to the coiled-coil region of the beta' subunit. The coiled-coil is a docking site for sigma factors on RNA polymerase, and evidence is presented that the binding of Fin and sigmaF to RNA polymerase is mutually exclusive. We propose that Fin functions by a mechanism distinct from that of classic sigma factor antagonists (anti-sigma factors), which bind directly to a target sigma factor to prevent its association with RNA polymerase, and instead functions to inhibit sigmaF by competing for binding to the beta' coiled-coil.
A novel RNA polymerase-binding protein that interacts with a sigma-factor docking site.,Wang Erickson AF, Deighan P, Chen S, Barrasso K, Garcia CP, Martinez-Lumbreras S, Alfano C, Krysztofinska EM, Thapaliya A, Camp AH, Isaacson RL, Hochschild A, Losick R Mol Microbiol. 2017 Aug;105(4):652-662. doi: 10.1111/mmi.13724. Epub 2017 Jun 19. PMID:28598017[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Carrasco B, Cozar MC, Lurz R, Alonso JC, Ayora S. Genetic recombination in Bacillus subtilis 168: contribution of Holliday junction processing functions in chromosome segregation. J Bacteriol. 2004 Sep;186(17):5557-66. PMID:15317759 doi:http://dx.doi.org/10.1128/JB.186.17.5557-5566.2004
- ↑ Camp AH, Wang AF, Losick R. A small protein required for the switch from {sigma}F to {sigma}G during sporulation in Bacillus subtilis. J Bacteriol. 2011 Jan;193(1):116-24. doi: 10.1128/JB.00949-10. Epub 2010 Oct 29. PMID:21037003 doi:http://dx.doi.org/10.1128/JB.00949-10
- ↑ Wang Erickson AF, Deighan P, Chen S, Barrasso K, Garcia CP, Martinez-Lumbreras S, Alfano C, Krysztofinska EM, Thapaliya A, Camp AH, Isaacson RL, Hochschild A, Losick R. A novel RNA polymerase-binding protein that interacts with a sigma-factor docking site. Mol Microbiol. 2017 Aug;105(4):652-662. doi: 10.1111/mmi.13724. Epub 2017 Jun 19. PMID:28598017 doi:http://dx.doi.org/10.1111/mmi.13724
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