TY  - JOUR
AU  - Wojtowicz, H.
AU  - Prochnicka-Chalufour, A.
AU  - de Amorim, G. C.
AU  - Roudenko, O.
AU  - Simenel, C.
AU  - Malki, I.
AU  - Pehau-Arnaudet, G.
AU  - Gubellini, F.
AU  - Koutsioumpas, Alexandros
AU  - Perez, J.
AU  - Delepelaire, P.
AU  - Delepierre, M.
AU  - Fronzes, R.
AU  - Izadi-Pruneyre, N.
TI  - Structural basis of the signalling through a bacterial membrane receptor HasR deciphered by an integrative approach
JO  - Biochemical journal
VL  - 473
IS  - 14
SN  - 1470-8728
CY  - London
PB  - Portland Press79505
M1  - FZJ-2016-04249
SP  - 2239 - 2248
PY  - 2016
AB  - 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.
LB  - PUB:(DE-HGF)16
UR  - <Go to ISI:>//WOS:000393707500022
C6  - pmid:27208170
DO  - DOI:10.1042/BCJ20160131
UR  - https://juser.fz-juelich.de/record/811935
ER  -