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Directrice de Recherche CNRS

Tel. : +33 (0)4 91 16 45 49
Fax : +33 (0)4 91 16 46 89

Equipe de recherche : Enzymologie des Systèmes Supramoléculaires

Our group is fascinated by the structural and functional properties of intrinsically disordered proteins (IDPs). During the last decade, a growing interest has focused on these particularly intriguing proteins, as they are functionally active, despite their lack of stable regular structure.
Intrinsically disordered regions can act as spacers to modulate the distance and the activity of different modules. This is typically what we observed in plurimodular cellulases and cellulosomes, which use this flexibility to adapt their structure to cellulose, a substrate highly recalcitrant to degradation. Other IDPs are involved in many molecular recognition processes that play crucial roles in the mechanisms of regulation of the cell cycle and metabolism. These latter proteins are called hubs because they can interact with many different partners and are implicated in a large network of interactions. No less than 30% of the proteins encoded by eukaryotic genomes contain long disordered regions. Interaction with their partners often leads to a drastic change in their structure and dynamics. We have developed an expertise in the study of these original proteins and of their mechanisms of action by combining a series of complementary biophysical techniques.
We are in particular expert in Small Angle X-ray Scattering (SAXS), a very powerful technique that provides crucial information on the conformational properties of flexible polypeptide chains and on their distribution of conformations. We use SAXS, in combination with data from X-ray crystallography, NMR, circular dichroism and molecular modelling, to assess the structure and dynamics of IDPs, involved in macromolecular assemblies, and/or that undergo large conformational changes upon interaction with their partner(s), etc. We are particularly interested in the proteins involved in the regulation of photosynthesis in microalgae such as Chlamydomonas reinhardtii and diatoms.

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44. Launay H., Barré P., Puppo C., Zhang Y, Manneville S., Gontero B., Receveur-Brechot V. (2018) Cryptic disorder out of disorder : encounter between conditionally disordered CP12 and glyceraldehyde-3-phosphate dehydrogenase, J Mol Biol, 430(8),1218-1234.
43. Badillo A, Receveur-Brechot V, Sarrazin S, Cantrelle FX, Delolme F, Fogeron ML, Molle J, Montserret R, Bockmann A, Bartenschlager R, Lohmann V, Lippens G, Ricard-Blum S, Hanoulle X, and Penin F. (2017) Overall structural model of NS5A protein from Hepatitis C virus and modulation by mutations confering resistance of HCV replication to cyclosporin A, Biochemistry, 56(24), 3029-3048.
42. Arias-Cartin R., Ceccaldi P., Schoepp-Cothenet B., Frick C., Blanc JM, Guigliarelli B., Walburger A., Grimaldi S. ; Friedrich T., Receveur-Brechot V., Magalon A. (2016) Redox cofactor insertion in prokaryotic molybdoenzymes occurs via a conserved folding mechanism, Scientific Reports, 6, 37743. doi:10.1038/srep37743. Pubmed ID : 27886223
41. Chundawat SPS, Paavola CD, Raman B, Nouailler N, Chan SL,. Mielenz JR, Receveur-Brechot V., Trent J, and Dale BE. (2016) Saccharification of thermochemically pretreated cellulosic biomass using native and engineered cellulosomal enzyme systems, Reaction Chemistry & Engineering, 1, 616-628. DOI : 10.1039/C6RE00172F.
40. Launay H., Barré P., Puppo C., Manneville S., Gontero B., Receveur-Brechot V.. (2016) Absence of residual structure in the intrinsically disordered regulatory protein CP12 in its reduced state. Biochem Biophys Res Commun, 477(1), 20-26. Pubmed ID : 27268235
39. Roblin P, Lebrun P, Rucktooa P, Dewitte F, Lens Z, Receveur-Brechot V, Raussens V, Villeret V, Bompard (2013) The structural organization of the N-terminus domain of SopB, a virulence factor of Salmonella, depends on the nature of its protein partners. Biochim Biophys Acta. 1834(12), 2564-2572.
Pubmed ID : 24075929
38. Czjzek M., Fierobe HP, Receveur-Bréchot V. (2012) Small angle X-ray scattering and crystallography, a winning combination for exploring the multi-modular organisation of cellulolytic macromolecular complexes, Methods in Enzymology, 510, 183-210. Review. Pubmed ID : 22608727
37. Receveur-Bréchot V. & Durand D. (2012) How random are intrinsically disordered proteins ? A Small Angle Scattering perspective. Curr Prot. Pept. Science, 13(1), 55-75. Current Protein and Peptide Science, Volume 13, Number 1, February 2012 , pp. 55-75. Pubmed ID : 22044150
36. Daughdrill GW, Kashtanov S, Stancik A, Hill SE, Helms G, Muschol M, Receveur-Brechot V., Ytreberg FM (2012) Understanding the Ensemble Structure of a Highly Extended Disordered Protein. Molecular Biosystems, 8 (1), 308-319. Pubmed ID : 21979461
35. Prudent R., Moucadel V., Sautel CF, Barette C., Lafanechere L., Receveur-Brechot V. and Cochet C. (2011) Targeting Protein Kinase CK2 with Allosteric in Vivo Potent Inhibitors, Oncotarget, 2(12), 997-1010. Pubmed ID : 22184283
34. Durand E., Waksman G., Receveur-Brechot V. (2011) Structural insights into the membrane-extracted dimeric form of the ATPase TraB from the Escherichia coli pKM101 conjugation system BMC Struct. Biol., 11:4. Pubmed ID : 21266026
33. Molinier AL*, Nouailler M*, Valette O, Tardif C, Receveur-Brechot V & Fierobe, HP (2011) Synergy, Structure and Conformational Flexibility of Hybrid Cellulosomes Displaying Various Inter-Cohesins Linkers. J. Mol. Biol.,405, 143-157. Pubmed ID : 20970432
32. Foucault M., Mayol K., Receveur-Bréchot V., Bussat M., Klinguer-Hamour C., Verrier B., Beck A., Haser R., Gouet P., Guillon C. (2010) UV and X-ray structural studies of a 101-residue long Tat protein from a HIV-1 primary isolate and of its mutated, detoxified, vaccine candidate. Proteins, 78 (6), 1441-1456. Pubmed ID : 20034112
31. Sonan GK, Receveur-Brechot V., Duez C, Czjzek M., Aghajari N, Haser R, and Gerday C (2007) The importance of the linker region in the adaptation to cold of the cellulase from the Antarctic bacterium Pseudoalteromonas haloplanktis A23., Biochem. J., 407 293-302. Pubmed ID : 17635108
30. Schoehn G, Vellieux F M D, Durá MA, Receveur-Bréchot V, Fabry CMS, Ruigrok RWH, Ebel C, Roussel A, Franzetti B (2006) Pyrococcus horikoshii TET1 peptidase can assemble into a tetrahedron or a large octahedral shell similar to viral capsids, J. Biol. Chem, 281 : 36327-36337. Pubmed ID : 16973604
29. Receveur-Bréchot V., Czjzek M., Barre A., Roussel A., Peumans W.J., Van Damme E.J.M., Rougé P. (2006) Crystal structure at 1.45-Å resolution of the major allergen endo-beta-1,3-glucanase of banana as a molecular basis for the latex-fruit syndrom, Proteins, 63 : 235-242. Pubmed ID : 16421930
28. Receveur-Bréchot V., Bourhis J.M., Uversky V., Canard B., Longhi S. (2006) Assessing protein disorder and induced folding. Review, Proteins, 62 : 24-45. Pubmed ID : 16287116
27. Hammel M., Fierobe H.P., Czjzek M., Kurkal V., Smith J.C., Bayer EA, Finet S., Receveur-Bréchot V. (2005) Structural basis of cellulosome efficiency explored by small angle X-ray scattering, J. Biol. Chem., 280 : 38562-38568. Pubmed ID : 16157599
26. Bourhis J.M., Receveur-Bréchot V., Zhang X., Oglesbee M., Buccellato M., Darbon H., Canard B., Finet S., Longhi S. (2005) The intrinsically disordered C-terminal domain of measles virus nucleoprotein interacts with the C-terminal domain of the measles virus phosphoprotein via two distinct sites and remains predominantly unfolded after binding, Protein Sci., 14:1975–1992. Pubmed ID : 16046624
25. Violot S., Aghajari N., Czjzek M., Feller G., Sonan GK., Gouet P., Gerday C., Haser R., Receveur-Bréchot V. (2005) Structural features of cold adaptation in a psychrophilic cellulase revealed by X-ray Diffraction and Small Angle X-ray Scattering, J. Mol. Biol. 348(5) 1211-24. Pubmed ID : 15854656
24. Durá M.A, Receveur-Brechot V., Andrieu JP, Ebel C., Schoehn G., Roussel A, Franzetti B. (2005) Characterization of a TET-like aminopeptidase complex from the hyperthermophilic archaeon Pyrococcus horikoshii, Biochemistry 44(9),3477-3486. Pubmed ID : 15736957
23. Graille M., Zhou CZ, Receveur-Bréchot V., Collinet B., Leulliot N., Declerck N., van Tilbeurgh H. (2005) Activation of the LicT transcriptional antiterminator by a domain swing/lock mechanism J. Biol. Chem. 280(15):14780-9. Pubmed ID : 15699035
22. Porciero S., Receveur-Bréchot V., Mori K., Franzetti B., Roussel A. (2005) Expression, purification, crystallization and preliminary crystallographic analysis of a deblocking amino peptidase from Pyrococcus horikoshii, Acta Cryst. F61, 239-242. doi:10.1107/S1744309105001910 Pubmed ID : 16511005
21. von Ossowski I., Eaton J.T., Czjzek M., Perkins S.J., Frandsen T.P., Schülein M., Panine P., Henrissat B., Receveur-Bréchot V. (2005) Protein disorder : Conformational distribution of a long flexible linker in a chimeric double cellulase, Biophys. J. ,88, 2823-2832. Pubmed ID : 15653742
20. Hammel M., Fierobe HP, Czjzek M., Finet S., Receveur-Bréchot V. (2004) Structural Insights into the Mechanism of Formation of Cellulosomes probed by Small Angle X-ray Scattering, J. Biol. Chem., 279, 55985-55994. Pubmed ID : 15502162
19. Bourhis J.M., Johansson K., Receveur-Bréchot V. , Oldfield C.J., Dunker K.A., Canard B., Longhi S. (2004) The C-terminal domain of measles virus nucleoprotein belongs to the class of intrinsically disordered proteins that fold upon binding to their physiological partner, Virus Research, 99, 157-167. Pubmed ID : 14749181
18. Dellisanti C.D., Spinelli S., Cambillau C., Findlay J.B.C., Zagalsky P.F., Finet S., Receveur-Bréchot V. (2003) Quaternary Structure of Alpha-Crustacyanin from Lobster as Seen by Small Angle X-Ray Scattering, FEBS Lett., 544, 189-193. Pubmed ID : 12782314
17. Longhi S., Receveur-Bréchot V., Karlin D., Johansson K., Darbon H., Bhella D., Yeo R., Finet S., Canard B. (2003) The C-terminal domain of the measles virus nucleoprotein is intrinsically disordered and folds upon binding to the C-terminal moiety of the phosphoprotein, J. Biol. Chem, 278, 18638-18648. Pubmed ID : 12621042
16. Receveur V., Czjzek M., Schülein M., Panine P., Henrissat B. (2002) Dimension, shape and conformational flexibility of a two-domain fungal cellulase in solution probed by small angle X-ray scattering J. Biol. Chem, 277, 40887-40892. Pubmed ID : 12186865
15. Karlin D., Longhi S., Receveur V., Canard B. (2002) The N-terminal domain of the Phosphoprotein of Morbilliviruses is natively unfolded, Virology, 296, 251-262. Pubmed ID : 12069524
14. Declerck N., Dutartre H., Receveur V., Dubois V., Royer C., Aymerich S., van Tilbeurgh H. (2001) Dimer Stabilization upon Activation of the transcriptional antiterminator LicT, J. Mol. Biol, 314 671-681. Pubmed ID : 11733988
13. Chamberlain AK., Receveur V., Spencer A., Redfield C., Dobson CM. (2001) Analysis of the Structure and Dynamics of Amyloidogenic Mutants of Human Lysozyme, Protein Science, 10 2525-2530. Pubmed ID : 11714920
12. Receveur V., Garcia P., Durand D., Vachette P., Desmadril M. (2000) Role of hydrophobic interactions in yeast phosphoglycerate kinase stability, Proteins, 38, 226-238. Pubmed ID : 10656268
11. Petrescu A.J., Calmettes P., Durand D., Receveur V., Smith J.C. (2000) Change in Backbone Torsion Angle Distribution on Protein Folding, Protein Sci 6:1129-1136. Pubmed ID : 10892806
10. Morozova-Roche L.A., Zurdo J., Spencer A., Noppe W., Receveur V., Archer D.B., Joniau M., Dobson C.M. (2000) Amyloid Fibril formation and seeding by wild-type human Lysozyme and its disease-related mutational variants, J. Struct. Biol.,130, 339-351.Pubmed ID : 10940237
9. D.M. Wilkins, S.B. Grimshaw, V. Receveur, C.M. Dobson, J.A. Jones, L.J. Smith (1999) Hydrodynamic radii of native and denatured proteins measured using pulse field gradient NMR techniques, Biochemistry 38, 16424-16431. Pubmed ID : 10600103
8. V. Receveur, D. Durand, M. Desmadril, P. Calmettes (1998) Repulsive intermolecular interactions in a denatured protein solution revealed by small angle neutron scattering, FEBS Letters 426, 57-61. Pubmed ID : 9598978
7. P. Garcia, F. Merola, V. Receveur, P. Minard, M. Desmadril (1998) Steady-state fluorescence and time-resolved fluorescence study of residual structures in an unfolded form of phosphoglycerate kinase from yeast, Biochemistry 37, 7444-7455. Pubmed ID : 9585558
6. A.J. Petrescu, V. Receveur, P. Calmettes, D. Durand, J.C. Smith (1998) Excluded volume effect on the configurational distribution of a strongly denatured protein, Protein Science 7, 1396-1403. Pubmed ID : 9655344
5. J. Smith, A. Lamy, M. Kataoka, J. Yunoki, A.J. Petrescu, V. Receveur, P. Calmettes, D Durand (1998) Motions in native and denatured proteins, Physica B, 241-243, 1110-1114.
4. V. Receveur, D. Durand, P. Calmettes, J.C. Smith, M. Desmadril, G. Coddens (1997) Picosecond dynamical changes in yeast phosphoglycerate kinase on denaturation probed by quasielastic neutron scattering, Proteins : Struct. Funct. Genet. 28, 380-387. Pubmed ID : 9223184
3. A.J. Petrescu, V. Receveur, P. Calmettes, D. Durand, M. Desmadril, B. Roux, J.C. Smith, (1997) Small angle neutron scattering of a strongly denatured protein : Analysis using random polymer theory, Biophys. J. 72, 335-342. Pubmed ID : 8994618
2. P. Calmettes, D. Durand, V. Receveur, M. Desmadril, P. Minard, R. Douillard (1995) Structure of phosphoglycerate kinase and beta-casein denatured in guanidinium chloride, Physica B 213&214, 754-756.
1. P. Calmettes, D. Durand, M. Desmadril, P. Minard, V. Receveur, J.C. Smith, (1994) How random is a highly denatured protein ?, Biophys. Chem., 53, 105-114. Pubmed ID : 17020841


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