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Cells are placed vertically in micro-fabricated cavities; cytokinetic rings of yeasts (schematically at the top) and mammalian cells (schematically at the bottom) are visible (yellow and green rings respectively). These structures are characterized by distinct collective dynamic of molecular motors.
© IGBMC / Team Daniel Riveline
July 1, 2016
The team of Daniel Riveline at IGBMC (CNRS, INSERM, University of Strasbourg) and at the Institute of Science and Supramolecular Engineering (ISIS, CNRS, University of Strasbourg), in collaboration with the team of Karsten Kruse (Saarland University, Germany) has revealed the mechanisms leading to physical separations of yeast and mammalian cells. These results are published in the journal Nature Communications, July 1st 2016.
Under normal condition (left), FMRP helps produce the Dgkk enzyme in neurons. In the fragile X situation, in the absence of FMRP (right), Dgkk is not sufficiently produced. Acting on Dgk enzymatic activity would be a way to correct the defects associated with the fragile X syndrome.
© IGBMC / Hervé Moine
July 11, 2016
A study supervised by Hervé Moine evidenced a pathogenic mechanism for fragile X syndrome. This genetic disease most often causes intellectual disabilities, behavioral problems and physical abnormalities. These results were published in the Proceedings of the National Academy of Sciences (PNAS) on May 27th.
Super-resolution image depicting DNA Double Strand Breaks (revealed by g-H2AX, the main DSB marker, in red) in centromeres (in green), localized around the DAPI-dense regions corresponding to pericentromeres.
July 7, 2016
The teams of Evi Soutoglou and Bernardo Reina-San-Martin have taken advantage of the CRISPR/Cas9 genome editing technology to identify the molecular mechanisms regulating the repair of double stranded DNA breaks (DSBs) arising in highly compacted chromatin (constitutive heterochromatin). These results are published on July 7th 2016 in Molecular Cell.
RNA pol I dimer is inactive and cannot bind to DNA because in this form both monomers mutually inhibit their active site. The binding Rrn3 promotes dissociation of the dimer by partnering with the dimerization interface, and allows the recruitment of the promoter of the ribosomal genes through interaction with the Core factor. Rrn3 dissociates when RNA Pol I transcribes the gene and the monomeric form released at the end of the gene tend to dimerize.
July 15, 2016
The team of Patrick Schultz at the IGBMC has unveiled the architecture of an activated form of RNA polymerase I (RNA Pol I) by cryo electron microscopy. This enzyme synthesizes a particular class of RNA which is necessary for the formation of ribosomes; the molecular machinery responsible for protein synthesis. The results are published in the journal Nature Communications, since July 15th.