ArticleScientific reports2020
Structural analysis and insight into effector binding of the niacin-responsive repressor NiaR from Bacillus halodurans.
Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 8 citations in OpenAlex.
- c-di-GMP regulates bacterial NAD biosynthesis via targeting the transcriptional repressor NadR.mBio · 2025Article
- The activation of the metal-containing regulatory protein NiaR from Thermotoga maritima by its effector, nicotinic acid.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2025Article
- Small molecule modulation of protein corona for deep plasma proteome profiling.Nature communications · 2024Article
- Deep Plasma Proteome Profiling by Modulating Single Nanoparticle Protein Corona with Small Molecules.bioRxiv : the preprint server for biology · 2024Article
- Niacinamide Antimicrobial Efficacy and Its Mode of Action via Microbial Cell Cycle Arrest.Microorganisms · 2024Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The niacin-responsive repressor, NiaR, is transcriptional repressor of certain nicotinamide adenine dinucleotide (NAD) biosynthetic genes in response to an increase in niacin levels. NAD is a vital molecule involved in various cellular redox reactions as an electron donor or electron acceptor. The NiaR family is conserved broadly in the Bacillus/Clostridium group, as well as in the Fusobacteria and Thermotogales lineages. The NiaR structure consists of two domains: an N-terminal DNA-binding domain, and a C-terminal regulation domain containing a metal-binding site. In this paper, we report the crystal structures of apo and niacin-bound forms of NiaR from Bacillus halodurans (BhNiaR). The analysis of metal-binding and niacin-binding sites through the apo and niacin-bound structures is described. Each N- and C-terminal domain structure of BhNiaR is almost identical with NiaR from Thermotoga maritima, but the overall domain arrangement is quite different. A zinc ion is fully occupied in each subunit with well-conserved residues in the C-terminal domain. Niacin is also located at a hydrophobic pocket near the zinc ion in the C-terminal domain.
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