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| | ==Crystal structure of TetR family protein Rv0078 in complex with DNA== | | ==Crystal structure of TetR family protein Rv0078 in complex with DNA== |
| - | <StructureSection load='6c31' size='340' side='right' caption='[[6c31]], [[Resolution|resolution]] 3.00Å' scene=''> | + | <StructureSection load='6c31' size='340' side='right'caption='[[6c31]], [[Resolution|resolution]] 3.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6c31]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Myctu Myctu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6C31 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6C31 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6c31]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6C31 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6C31 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5wm9|5wm9]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">LH57_00450 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83332 MYCTU])</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=6c31 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6c31 OCA], [https://pdbe.org/6c31 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6c31 RCSB], [https://www.ebi.ac.uk/pdbsum/6c31 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6c31 ProSAT]</span></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=6c31 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6c31 OCA], [http://pdbe.org/6c31 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6c31 RCSB], [http://www.ebi.ac.uk/pdbsum/6c31 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6c31 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/O53623_MYCTU O53623_MYCTU] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 6c31" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6c31" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Tetracycline repressor protein 3D structures|Tetracycline repressor protein 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Myctu]] | + | [[Category: Large Structures]] |
| - | [[Category: Hsu, H C]] | + | [[Category: Mycobacterium tuberculosis H37Rv]] |
| - | [[Category: Li, H]] | + | [[Category: Hsu HC]] |
| - | [[Category: Dna]] | + | [[Category: Li H]] |
| - | [[Category: Dna binding protein-dna complex]]
| + | |
| - | [[Category: Rv0078]]
| + | |
| - | [[Category: Tetr family]]
| + | |
| Structural highlights
Function
O53623_MYCTU
Publication Abstract from PubMed
It was recently reported that the human-exclusive pathogen Mycobacterium tuberculosis secretes cytokinins, which had only been known as plant hormones. While cytokinins are well-established, adenine-based signaling molecules in plants, they have never been shown to participate in signal transduction in other kingdoms of life. M. tuberculosis is not known to interact with plants. Therefore, we tested the hypothesis that cytokinins trigger transcriptional changes within this bacterial species. Here, we show cytokinins induced the strong expression of the M. tuberculosis gene Rv0077c. We found that Rv0077c expression is repressed by a TetR-like transcriptional repressor, Rv0078. Strikingly, cytokinin-induced expression of Rv0077c resulted in a loss of acid-fast staining of M. tuberculosis While acid-fast staining is thought to be associated with changes in the bacterial cell envelope and virulence, Rv0077c-induced loss of acid-fastness did not affect antibiotic susceptibility or attenuate bacterial growth in mice, consistent with an unaltered mycolic acid profile of Rv0077c-expressing cells. Collectively, these findings show cytokinins signal transcriptional changes that can affect M. tuberculosis acid-fastness and that cytokinin signaling is no longer limited to the kingdom Plantae.IMPORTANCE Cytokinins have only previously been known as plant hormones. The discovery that they can be used as signaling molecules outside of plants broadens the repertoire of small molecules that can potentially affect gene expression in all domains of life.
Cytokinin Signaling in Mycobacterium tuberculosis.,Samanovic MI, Hsu HC, Jones MB, Jones V, McNeil MR, Becker SH, Jordan AT, Strnad M, Xu C, Jackson M, Li H, Darwin KH MBio. 2018 Jun 19;9(3). pii: mBio.00989-18. doi: 10.1128/mBio.00989-18. PMID:29921668[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Samanovic MI, Hsu HC, Jones MB, Jones V, McNeil MR, Becker SH, Jordan AT, Strnad M, Xu C, Jackson M, Li H, Darwin KH. Cytokinin Signaling in Mycobacterium tuberculosis. MBio. 2018 Jun 19;9(3). pii: mBio.00989-18. doi: 10.1128/mBio.00989-18. PMID:29921668 doi:http://dx.doi.org/10.1128/mBio.00989-18
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