Abstract:
:NikR is a transcriptional metalloregulator central in the mandatory response to acidity of Helicobacter pylori that controls the expression of numerous genes by binding to specific promoter regions. NikR/DNA interactions were proposed to rely on protein activation by Ni(II) binding to high-affinity (HA) and possibly secondary external (X) sites. We describe a biochemical characterization of HpNikR mutants that shows that the HA sites are essential but not sufficient for DNA binding, while the secondary external (X) sites and residues from the HpNikR dimer-dimer interface are important for DNA binding. We show that a second metal is necessary for HpNikR/DNA binding, but only to some promoters. Small-angle X-ray scattering shows that HpNikR adopts a defined conformation in solution, resembling the cis-conformation and suggests that nickel does not trigger large conformational changes in HpNikR. The crystal structures of selected mutants identify the effects of each mutation on HpNikR structure. This study unravels key structural features from which we derive a model for HpNikR activation where: (i) HA sites and an hydrogen bond network are required for DNA binding and (ii) metallation of a unique secondary external site (X) modulates HpNikR DNA binding to low-affinity promoters by disruption of a salt bridge.
journal_name
Nucleic Acids Resjournal_title
Nucleic acids researchauthors
Bahlawane C,Dian C,Muller C,Round A,Fauquant C,Schauer K,de Reuse H,Terradot L,Michaud-Soret Idoi
10.1093/nar/gkp1216subject
Has Abstractpub_date
2010-05-01 00:00:00pages
3106-18issue
9eissn
0305-1048issn
1362-4962pii
gkp1216journal_volume
38pub_type
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