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| Content Provider | Springer Nature Link |
|---|---|
| Author | Stoof, Jeroen Kuipers, Ernst J. Vliet, Arud H. M. |
| Copyright Year | 2009 |
| Abstract | The NikR protein is a nickel-responsive regulator, which in the gastric pathogen Helicobacter pylori controls expression of nickel-transporters and the nickel-cofactored urease acid resistance determinant. Although NikR-DNA interaction has been well studied, the Helicobacter NikR operator site remains poorly defined. In this study we have identified the NikR operators in the promoters of two inversely nickel-regulated urease operons (ureAB and ureA2B2) in the ferret pathogen Helicobacter mustelae, and have used bioinformatic approaches for the prediction of putative NikR operators in the genomes of four urease-positive Helicobacter species. Helicobacter mustelae NikR bound to the ureA2 promoter to a sequence overlapping with the −35 promoter region, leading to repression. In contrast, NikR binding to a site far upstream of the canonical σ80 promoter in the H. mustelae ureA promoter resulted in transcriptional induction, similar to the situation in H. pylori. Using H. pylori NikR operators and the newly identified H. mustelae NikR operators a new consensus sequence was generated (TRWYA-N15-TRWYA), which was used to screen the genomes of four urease-positive Helicobacter species (H. mustelae, H. pylori, H. acinonychis and H. hepaticus) for putative NikR-regulated promoters. One of these novel putative NikR-regulated promoters in H. mustelae is located upstream of a putative TonB-dependent outer membrane protein designated NikH, which displayed nickel-responsive expression. Insertional inactivation of the nikH gene in H. mustelae resulted in a significant decrease in urease activity, and this phenotype was complemented by nickel-supplementation of the growth medium, suggesting a function for NikH in nickel transport accross the outer membrane. In conclusion, the H. mustelae NikR regulator directly controls nickel-responsive regulation of ureases and metal transporters. The improved consensus NikR operator sequence allows the prediction of additional NikR targets in Helicobacter genomes, as demonstrated by the identification of a new nickel-repressed outer membrane protein in H. mustelae. |
| Starting Page | 145 |
| Ending Page | 159 |
| Page Count | 15 |
| File Format | |
| ISSN | 09660844 |
| Journal | BioMetals |
| Volume Number | 23 |
| Issue Number | 1 |
| e-ISSN | 15728773 |
| Language | English |
| Publisher | Springer Netherlands |
| Publisher Date | 2009-11-06 |
| Publisher Place | Dordrecht |
| Access Restriction | One Nation One Subscription (ONOS) |
| Subject Keyword | Nickel-responsive gene regulation Nickel uptake NikR repressor Helicobacter Physical Chemistry Biochemistry |
| Content Type | Text |
| Resource Type | Article |
| Subject | Metals and Alloys Biochemistry, Genetics and Molecular Biology Biomaterials Agricultural and Biological Sciences |
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