ArticleThe Biochemical journal2016
Structural basis of the signalling through a bacterial membrane receptor HasR deciphered by an integrative approach.
Article in The Biochemical journal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 18 citations in OpenAlex.
- Mechanism of MCUB-Dependent Inhibition of Mitochondrial Calcium Uptake.Journal of cellular physiology · 2025Article
- Article
- Extracellular haem utilization by the opportunistic pathogen Pseudomonas aeruginosa and its role in virulence and pathogenesis.Advances in microbial physiology · 2021Article
- Cell Communications among Microorganisms, Plants, and Animals: Origin, Evolution, and Interplays.International journal of molecular sciences · 2020Review
- Gallium(III)-Salophen as a Dual Inhibitor ofACS infectious diseases · 2020Article
- Low-Resolution Structure of Detergent-Solubilized Membrane Proteins from Small-Angle Scattering Data.Biophysical journal · 2017Article
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Authors and funding
14 authors at 6 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bacteria use diverse signalling pathways to adapt gene expression to external stimuli. In Gram-negative bacteria, the binding of scarce nutrients to membrane transporters triggers a signalling process that up-regulates the expression of genes of various functions, from uptake of nutrient to production of virulence factors. Although proteins involved in this process have been identified, signal transduction through this family of transporters is not well understood. In the present study, using an integrative approach (EM, SAXS, X-ray crystallography and NMR), we have studied the structure of the haem transporter HasR captured in two stages of the signalling process, i.e. before and after the arrival of signalling activators (haem and its carrier protein). We show for the first time that the HasR domain responsible for signal transfer: (i) is highly flexible in two stages of signalling; (ii) extends into the periplasm at approximately 70-90 Å (1 Å=0.1 nm) from the HasR β-barrel; and (iii) exhibits local conformational changes in response to the arrival of signalling activators. These features would favour the signal transfer from HasR to its cytoplasmic membrane partners.
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