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Apply for fellowship ” Heme import in bacteria: structural studies of transmembrane protein complexes ” CALL2

PI: Valérie Biou, Nathalie Dautin, Philippe Delepelaire

Iron is necessary for bacterial growth and is imported via specific membrane systems that span the two membranes of gram-negative bacteria.
The present post-doctoral project aims at deciphering the mechanism of heme import in two different bacterial heme acquisition systems:
A) The Heme Acquisition System (Has) from Serratia marcescens has already been extensively studied by our team (Biou et al., 2021; Wojtowicz et al., 2016; Zambolin et al., 2016), see figure 1;
B) the Hemoglobin-haptoglobin binding proteins (Hgps), a family of TonB-dependent transporters from Haemophilus influenzae able to import heme from the human hemoglobin-haptoglobin complex.
These projects involve multi-protein expression and purification, cryo-electron microscopy (cryo-EM) and in vivo studies to elucidate their mechanisms.
Our laboratory is a leader in membrane protein biochemistry and biophysics and has access to several cryo-TEM microscopes including those of the Pasteur institute and of the ESRF in Grenoble. We have use the computing cluster at the Theoretical Biophysics lab at the IBPC for data processing.
We are seeking a highly motivated post-doc with either experience in single particle cryo-EM sample preparation, data collection and processing and/or a strong knowledge of membrane protein biochemistry.



Biou, V., Adaixo, R.J.D., Chami, M., Coureux, P.-D., Laurent, B., Ntsogo, Y., Amorim, G.C. de, Izadi-Pruneyre, N., Malosse, C., Chamot-Rooke, J., Stahlberg, H., Delepelaire, P., 2021. Functional and structural characterization of Serratia marcescens ExbB: determinants of the interaction with HasB/TonB. bioRxiv 2021.04.21.440815.
Wojtowicz, H., Prochnicka-Chalufour, A., de Amorim, G.C., Roudenko, O., Simenel, C., Malki, I., Pehau-Arnaudet, G., Gubellini, F., Koutsioubas, A., Perez, J., Delepelaire, P., Delepierre, M., Fronzes, R., Izadi-Pruneyre, N., 2016. Structural basis of the signalling through a bacterial membrane receptor HasR deciphered by an integrative approach. Biochem. J. 473, 2239–2248.
Zambolin, S., Clantin, B., Chami, M., Hoos, S., Haouz, A., Villeret, V., Delepelaire, P., 2016. Structural basis for haem piracy from host haemopexin by Haemophilus influenzae. Nat. Commun. 7, 11590.


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This project is funded by the European Union’s Horizon 2020 Research and Innovation Programme under the Marie Skłodowska-Curie actions (grant agreement No 101034407).