The <em>Xanthomonas</em> RaxH-RaxR Two-Component Regulatory System Is Orthologous to the Zinc-Responsive <em>Pseudomonas</em> ColS-ColR System
Genome sequence comparisons to infer likely gene functions require accurate ortholog assignments. In <i>Pseudomonas</i> spp., the sensor-regulator ColS-ColR two-component regulatory system responds to zinc and other metals to control certain membrane-related functions, including lipid A...
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| Format: | Article |
| Language: | English |
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MDPI AG
2021-07-01
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| Series: | Microorganisms |
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| Online Access: | https://www.mdpi.com/2076-2607/9/7/1458 |
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| author | Valley Stewart Pamela C. Ronald |
| author_facet | Valley Stewart Pamela C. Ronald |
| author_sort | Valley Stewart |
| collection | DOAJ |
| description | Genome sequence comparisons to infer likely gene functions require accurate ortholog assignments. In <i>Pseudomonas</i> spp., the sensor-regulator ColS-ColR two-component regulatory system responds to zinc and other metals to control certain membrane-related functions, including lipid A remodeling. In <i>Xanthomonas</i> spp., three different two-component regulatory systems, RaxH-RaxR, VgrS-VgrR, and DetS-DetR, have been denoted as ColS-ColR in several different genome annotations and publications. To clarify these assignments, we compared the sensor periplasmic domain sequences and found that those from <i>Pseudomonas</i> ColS and <i>Xanthomonas</i> RaxH share a similar size as well as the location of a Glu-X-X-Glu metal ion-binding motif. Furthermore, we determined that three genes adjacent to <i>raxRH</i> are predicted to encode enzymes that remodel the lipid A component of lipopolysaccharide. The modifications catalyzed by lipid A phosphoethanolamine transferase (EptA) and lipid A 1-phosphatase (LpxE) previously were detected in lipid A from multiple <i>Xanthomonas</i> spp. The third gene encodes a predicted lipid A glycosyl transferase (ArnT). Together, these results indicate that the <i>Xanthomonas</i> RaxH-RaxR system is orthologous to the <i>Pseudomonas</i> ColS-ColR system that regulates lipid A remodeling. To avoid future confusion, we recommend that the terms ColS and ColR no longer be applied to <i>Xanthomonas</i> spp., and that the Vgr, Rax, and Det designations be used instead. |
| first_indexed | 2024-03-10T09:31:52Z |
| format | Article |
| id | doaj.art-d3ed7c5f4a9e4898b56f34ac5f8873cf |
| institution | Directory Open Access Journal |
| issn | 2076-2607 |
| language | English |
| last_indexed | 2024-03-10T09:31:52Z |
| publishDate | 2021-07-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Microorganisms |
| spelling | doaj.art-d3ed7c5f4a9e4898b56f34ac5f8873cf2023-11-22T04:26:01ZengMDPI AGMicroorganisms2076-26072021-07-0197145810.3390/microorganisms9071458The <em>Xanthomonas</em> RaxH-RaxR Two-Component Regulatory System Is Orthologous to the Zinc-Responsive <em>Pseudomonas</em> ColS-ColR SystemValley Stewart0Pamela C. Ronald1Department of Microbiology & Molecular Genetics, University of California, Davis, CA 95616, USADepartment of Plant Pathology and Genome Center, University of California, Davis, CA 95616, USAGenome sequence comparisons to infer likely gene functions require accurate ortholog assignments. In <i>Pseudomonas</i> spp., the sensor-regulator ColS-ColR two-component regulatory system responds to zinc and other metals to control certain membrane-related functions, including lipid A remodeling. In <i>Xanthomonas</i> spp., three different two-component regulatory systems, RaxH-RaxR, VgrS-VgrR, and DetS-DetR, have been denoted as ColS-ColR in several different genome annotations and publications. To clarify these assignments, we compared the sensor periplasmic domain sequences and found that those from <i>Pseudomonas</i> ColS and <i>Xanthomonas</i> RaxH share a similar size as well as the location of a Glu-X-X-Glu metal ion-binding motif. Furthermore, we determined that three genes adjacent to <i>raxRH</i> are predicted to encode enzymes that remodel the lipid A component of lipopolysaccharide. The modifications catalyzed by lipid A phosphoethanolamine transferase (EptA) and lipid A 1-phosphatase (LpxE) previously were detected in lipid A from multiple <i>Xanthomonas</i> spp. The third gene encodes a predicted lipid A glycosyl transferase (ArnT). Together, these results indicate that the <i>Xanthomonas</i> RaxH-RaxR system is orthologous to the <i>Pseudomonas</i> ColS-ColR system that regulates lipid A remodeling. To avoid future confusion, we recommend that the terms ColS and ColR no longer be applied to <i>Xanthomonas</i> spp., and that the Vgr, Rax, and Det designations be used instead.https://www.mdpi.com/2076-2607/9/7/1458ColS-ColRRaxH-RaxRVgrS-VgrRlipid A remodelinglipid A phosphoethanolamine transferaselipid A 1-phosphatase |
| spellingShingle | Valley Stewart Pamela C. Ronald The <em>Xanthomonas</em> RaxH-RaxR Two-Component Regulatory System Is Orthologous to the Zinc-Responsive <em>Pseudomonas</em> ColS-ColR System Microorganisms ColS-ColR RaxH-RaxR VgrS-VgrR lipid A remodeling lipid A phosphoethanolamine transferase lipid A 1-phosphatase |
| title | The <em>Xanthomonas</em> RaxH-RaxR Two-Component Regulatory System Is Orthologous to the Zinc-Responsive <em>Pseudomonas</em> ColS-ColR System |
| title_full | The <em>Xanthomonas</em> RaxH-RaxR Two-Component Regulatory System Is Orthologous to the Zinc-Responsive <em>Pseudomonas</em> ColS-ColR System |
| title_fullStr | The <em>Xanthomonas</em> RaxH-RaxR Two-Component Regulatory System Is Orthologous to the Zinc-Responsive <em>Pseudomonas</em> ColS-ColR System |
| title_full_unstemmed | The <em>Xanthomonas</em> RaxH-RaxR Two-Component Regulatory System Is Orthologous to the Zinc-Responsive <em>Pseudomonas</em> ColS-ColR System |
| title_short | The <em>Xanthomonas</em> RaxH-RaxR Two-Component Regulatory System Is Orthologous to the Zinc-Responsive <em>Pseudomonas</em> ColS-ColR System |
| title_sort | em xanthomonas em raxh raxr two component regulatory system is orthologous to the zinc responsive em pseudomonas em cols colr system |
| topic | ColS-ColR RaxH-RaxR VgrS-VgrR lipid A remodeling lipid A phosphoethanolamine transferase lipid A 1-phosphatase |
| url | https://www.mdpi.com/2076-2607/9/7/1458 |
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