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© Institut Pasteur
Cells infected for 24 hrs with C. Trachomatis. The cell nuclei are labelled in blue, the bacteria appear yellow, within the inclusion lumen. A bacterial protein secreted out the inclusion into the host cytoplasm id labelled in red.
Publication : The Biochemical journal

Structural basis of the signalling through a bacterial membrane receptor HasR deciphered by an integrative approach

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in The Biochemical journal - 13 May 2016

Wojtowicz H, Prochnicka-Chalufour A, de Amorim GC, Roudenko O, Simenel C, Malki I, Pehau-Arnaudet G, Gubellini F, Koutsioubas A, Pérez J, Delepelaire P, Delepierre M, Fronzes R, Izadi-Pruneyre N

Link to Pubmed [PMID] – 27208170

Biochem. J. 2016 07;473(14):2239-48

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.

https://www.ncbi.nlm.nih.gov/pubmed/27208170