Institut de Biologie StructuraleGrenoble / France

Contact person(s) related to this article / PETOSA Carlo



Team leader: Carlo Petosa

Our team is broadly interested in understanding the molecular mechanisms that underlie infectious disease. Current work focuses on:

- Nucleocytoplasmic transport of HIV proteins
- Activation of Epstein-Barr virus lytic infection

The approach is to study the structure and function of key proteins involved in these processes using X-ray crystallography and complementary techniques. The long-term goal is to use the insights gained to develop new medically relevant molecules for the treatment and prevention of disease.

Key Words:

HIV, Epstein-Barr Virus, nuclear transport, lytic replication


- Protein expression and purification
- Biochemical and biophysical characterization of macromolecular complexes
- X-ray crystallography
- Electron microscopy

Team members:

- Fabienne Hans, Lecturer
- Flore Mietton, Post-doctoral fellow
- Marjolaine Noirclerc-Savoye, Research Engineer
- Mizar Oliva, Ph.D. student
- Simon Harris, Master’s student
- Edoardo Cellupica, Master’s student


Goudarzi A, Zhang D, Huang H, Barral S, Kwon O, Qi S, Tang Z, Buchou T, Vitte AL, He T, Cheng Z, Montellier E, Gaucher J, Curtet S, Debernardi A, Charbonnier G, Puthier D, Petosa P, Panne D, Rousseaux S, Roeder RG, Zhao Y, Khochbin S (2016). Dynamic competing histone H4 K5K8 acetylation and butyrylation are hallmarks of highly active gene promoters. Mol Cell 62:169-180

Meyer PM, Socias S, Key J, Ransey E, Tjon E, Maia F, Buschiazzo A, Lei M, Botka C, Withrow J, Neau D, Rajashankar K, Anderson K, Baxter RH, Blacklow SC, Boggon TJ, Bonvin AMJJ, Borek D, Brett TJ, Caflisch A, Chang C-I, Chazin WJ, Corbett KD, Cosgrove MS, Crosson S, Dhe-Paganon S, Di Cera E, Drennan C, Eck M, Eichman BF, Fan QR, Ferré-D’Amaré AR, Fraser JS, Fromme JC, Garcia KC, Gaudet R, Gong P, Harrison SC, Heldwein EE, Jia Z, Keenan RJ, Kruse AC, Kvansakul M, McLellan JS, Modis Y, Otwinowski Z, Pai EF, Pereira P, Petosa C, Raman CS, Rapoport TA, Roll-Mecak A, Rosen MK, Rudenko G, Schlessinger J, Schwartz TU, Shamoo Y, Sondermann H, Tao YJ, Tolia N, Tsodikov OV, Westover KD, Wu H, Foster I, Maia FRNC, Gonen T, Kirchausen T, Diederichs K, Crosas M, Sliz P. (2016) Data publication with the structural biology data grid supports live analysis. Nature Comm. 7:10882

Ferri E, Petosa C, McKenna CE. (2016) Bromodomains: structure, function and pharmacology of inhibition. Biochem Pharmacol 106:1-18.

Morozumi Y, Boussouar F, Tan M, Chaikuad A, Jamshidikia M, Colak G, He H, Nie L, Petosa C, de Dieuleveult, Curtet S, Vitte AL, Schweifer N, Gianni D, Gut M, Guardiola P, Rousseaux S, Gérard M, Knapp S, Zhao Y, Khochbin S.(2015) Atad2 is a generalist facilitator of chromatin dynamics in embryonic stem cells. J Mol Cell Biol Oct 12. pii: mjv060

Boeri Erba E, Petosa C. (2015) The role of native mass spectrometry in characterizing the structure and dynamics of macromolecular assemblies. Protein Sci. 24:1176-92.

Dian C, Bernaudat F, Langer K, Oliva MF, Fornerod M, Schoehn G, Müller CW, Petosa C. (2013) Structure of a truncation mutant of the nuclear export factor CRM1 provides insights into the auto-inhibitory role of its C-terminal helix. Structure. 21:1338-1349.

Montellier E, Boussouar F, Rousseaux S, Zhang K, Buchou T, Fenaille F, Shiota H, Debernardi A, Héry P, Holota H, Lopez F, Guardiola P, Pernet K, Imbert J, Petosa C, Tan M, Zhao Y, Gérard M, Khochbin S. (2013) Chromatin-to-nucleoprotamine transition is controlled by the histone H2B variant TH2B. Genes Dev 27:1680-1692

Emadali A, Rousseaux S, Bruder-Costa J, Rome C, Duley S, Hamaidia S, Betton P, Debernardi A, Leroux D, Bernay B, Kieffer-Jaquinod S, Combes F, Ferri E, McKenna CE, Petosa C, Bruley C, Garin J, Ferro M, Gressin R, Callanan MB, Khochbin S. (2013) Identification of a novel BET bromodomain inhibitor-sensitive, gene regulatory circuit that controls Rituximab response and tumour growth in aggressive lymphoid cancers. EMBO Mol Med 5:1180-1195.

Perrakis A, Musacchio A, Cusack S, Petosa C. (2011) Investigating a macromolecular complex: The toolkit of methods. J Struct Biol. 175:106-12.

Langer K, Dian C, Rybin V, Müller CW, Petosa C. (2011) Insights into the function of the CRM1 cofactor RanBP3 from the structure of its Ran-binding domain. PLoS One 6(2):e17011.

Morinière J, Rousseaux S, Steuerwald U, Soler-López M, Curtet S, Vitte AL, Govin J, Gaucher J, Sadoul K, Hart DJ, Krijgsveld J, Khochbin S, Müller CW and Petosa C. (2009) Cooperative binding of two acetylation marks on a histone tail by a single bromodomain. Nature 461: 664-668

Karlsson QH, Schelcher C, Verrall E, Petosa C, Sinclair AJ. (2008) Methylated DNA recognition during the reversal of epigenetic silencing is regulated by cysteine and serine residues in the Epstein-Barr virus lytic switch protein. PLoS Pathog. 4(3):e1000005.

Petosa C, Morand P, Baudin F, Moulin M, Artero JB, Müller CW. (2006) Structural basis of lytic cycle activation by the Epstein-Barr virus ZEBRA protein. Mol. Cell 21:565-72.

Petosa, C., Schoehn, G., Askjaer, P., Bauer, U., Moulin, M., Steuerwald, U., Soler-López, M., Baudin, F., Mattaj, I.W., Müller, C.W. (2004) Architecture of CRM1/Exportin1 suggests how cooperativity is achieved during formation of a nuclear export complex. Mol. Cell 16:761-775.