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CGM - Department Genes Expression

RNA structure and dynamics

Group leader: Dominique FOURMY

ligne séparation   Last update: 13-Mar-2012

 

portrait des membres de l'équipe

Our team

Sylvie Auxilien, Engineer (1)

Nicolas Fiszman, PhD student (Institut d’Optique/CGM)

Dominique Fourmy, Researcher CNRS (4)

Henri Grosjean, Emeritus Researcher

Maho Okuda, PhD student

Raja Rekik, Master2 Student

Chie Tomikawa, Postdoctoral fellow (2)

Hélène Walbott, Postdoctoral fellow (5)

Satoko Yoshizawa, Researcher CNRS (3)

Our address

CNRS

Centre de Génétique Moléculaire

Avenue de la Terrasse - Bât. 24

91198 GIF-SUR-YVETTE Cedex

FRANCE

Phone: 33 (0)1 69 82 38 84

 

Research interests

short movie showing the model of SelB interaction with the ribosome

Model of SelB interaction with the ribosome (N. Soler)

Our team was created at CGM in September 2010. We are working at the interface of several disciplines. Our current work focuses on understanding protein synthesis using molecular and structural approaches with some new developments in nanotechnology. For eukaryotes, protein synthesis is mainly regulated at the step of initiation rather than during the phases of elongation and termination. This mechanism allows a strict control of gene expression. Translation initiation is a complex process where more than 10 factors are involved. We are investigating the mechanism of action of some of these factors and how they regulate initiation. During elongation the ribosome encounters some sequences that trigger a shift of its reading frame, a mechanism that remains to be clarified. Deciphering the molecular details of frameshifting will help to understand how the ribosome works. As the newly synthesized polypeptide exits from the ribosome, cotranslational events occur to mature the new protein. We are using fluorescent tools to characterize the interaction of some of the polypeptide maturation factors with the ribosome. More importantly it is essential to characterize translation in live cells and we are developing new tools toward this goal. Ribosome is essential to life and understanding its function at the molecular level will impact biology and medicine. Our study of translation is linked with cancer and cell infection by retroviruses.

 

Selected publications

Kawano, R., Osaki, T., Sasaki, H., Takinoue, M., Yoshizawa, S., and Takeuchi, S. (2011) Rapid Detection of a Cocaine-Binding Aptamer Using Biological Nanopores on a Chip. J Am Chem Soc, 133 (22) 8474-7.

White, K. H., Orzechowski, M., Fourmy, D., and Visscher, K.(2011) Mechanical unfolding of the Beet Western Yellow Virus -1 frameshift signal. J Am Chem Soc, 133 (25) 9775-82.

Auxilien, S., Rasmussen, A., Rose, S., Brochier-Armanet, C., Husson, C., Fourmy, D., Grosjean, H. and Douthwaite, S. (2011) Specificity shifts in the rRNA and tRNA nucleotide targets of archaeal and bacterial m5U methyltransferases. RNA, 17, 45-53.

Ginet, P., Montagne, K., Akiyamaa, S., Rajabpoura, A., Taniguchi, A., Fujii, T., Sakai, Y., Kim, B., Fourmy, D. and Volz, S.(2011) Towards Single Cell Heat Shock Response by Accurate Control on Thermal Confinement with an On-Chip Microwire Electrode. Lab on Chip , 11, 1513-1520.

Yoshizawa S, and Böck A. (2009) The many levels of control on bacteial selenoprotein synthesis. BBA, 1790, 1404-1414.

Ota S, Yoshizawa S, and Takeuchi S. (2009) Microfluidic formation of monodisperse, cell-sized and unilamellar vesicles.  Angewandte Chemie (International ed.), 48, 6533-6537.

Mazauric M.H., Seol.Y, Yoshizawa S., Visscher K. and Fourmy D. (2009) Interaction of the HIV-1 frameshift signal with the ribosome. Nucl Ac Res, 37, 7654-7664.

Mazauric M.H., Leroy J.L., Visscher K., Yoshizawa S. and Fourmy D. (2009) Footprinting analysis of BWYV pseudoknot-ribosome complexes. RNA, 15, 1775-1786.

Soler N., Fourmy D. and Yoshizawa S. (2007) Structural basis for a molecular switch in winged-helix domains of elongation factor selB. J Mol Biol, 370, 728-741.

Yoshizawa S. Rasubala L., Ose T., Kohda D., Fourmy, D., and Maenaka K. (2005) Structural basis for messenger RNA recognition by elongation factor SelB. Nat StrucMol Biol, 12, 198-203.

All the publications

 

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