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Laboratoire de Biologie Moléculaire Eucaryote

UMR 5099
Director: Pierre-Emmanuel Gleizes


The Laboratory of Eukaryotic Molecular Biology (LBME), a joint Université Paul Sabatier- CNRS unit (UMR 5099), is located on the University of Toulouse-Paul Sabatier campus in the IBCG building. The LBME is part of the Center for Integrative Biology in Toulouse (CBI Toulouse).

Research projects by the seven groups/teams of the LBME aim at understanding the mechanisms of genetic and epigenetic control of gene expression in eukaryotes. LBME activities evolve around two major themes:

  • The structural and functional characterization of nuclear and nucleolar ribonucleoprotein particles (pre-ribosomes, snoRNPs, scaRNPs, 7SK…)
  • Dynamics of chromosome structure and chromatin, in the context of gene transcription, homologous recombination and proliferation.

All projects are basic research and may elucidate the molecular basis of different pathologies including the Prader-Willi syndrome, the Blackfan-Diamond anemia, Dyskeratosis congenita and Cancer.

Research questions are addressed at different scales in a large number of model systems from single molecules to whole organisms (yeast, mouse and drosophila), including cell culture of primary or transformed cell lines. The LBME is leader in the study of nucleic acid/protein complexes using genetic, molecular biology, biochemistry, genomics, cell (fluorescence microscopy) and structural biology (cryo electronic microscopy) approaches.






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News Archives


    From June 1st til June 12th 2012, the IBCG (institute which houses both the LBME and the LMGM) participated in the challenge "Let's go there by bike!". The aim was to encourage the IBCG staff to prefer coming at work on their bicycle rather than taking the car.

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  • Impact of nucleosome interaction on Reptin/ Pontin oligomerization and activities

    AAA+ Pontin and Reptin are the main components of chromatin remodeling complexes. Up to now, no link has been defined between their in vivo functions and their biochemical properties. Researchers from the LBME has recently identified and characterized an interaction with the nucleosome that regulates both enzymatic activities and oligomerization assemblies of Pontin/Reptin. Their results establish that these proteins might generate a molecular loading platform on chromatin by coordinating different sets of interacting proteins through changes in their oligomerization state.


  • LBME’s scientific retreat at Saissac

    Every two years, the LBME organizes a "scientific retreat" outside the lab. This year, this internal meeting took place at Saissac on October 2nd and 3rd : two days of seminars, poster sessions, scientific exchange and round tables mixing science and friendliness.

  • Rcl1p and Bms1p: a vital partnership in the early stages of ribosome synthesis

    Within the pre-ribosomal particles, Rcl1p is a ribonuclease that catalyzes a crucial pre-rRNA cleavage event required for the synthesis of the 18S rRNA and the maturation of the small ribosomal subunit. Rcl1p interacts with the GTPase Bms1p that probably regulates its activity. The group headed by Anthony Henras and Yves Henry, in collaboration with the group of Sébastien Fribourg (IECB, Bordeaux) could identify the residues of Rcl1p involved in the interaction with Bms1p. Their results show that the Bms1p-Rcl1p interaction is essential for the production of the small ribosomal subunit and they suggest that GTP binding or hydrolysis by Bms1p induces conformational changes in the Rcl1p-Bms1p complex allowing pre-rRNA cleavage by Rcl1p.


  • The 2014 DBA Pioneer Award to Pierre-Emmanuel Gleizes

    The American Diamond-Blackfan Anemia Foundation (dbafoundation.org) has awarded its 2014 DBA Pioneer Award to Pierre-Emmanuel Gleizes for his work on ribosomal proteins and DBA gene discovery. The Gleizes group has been studying the functional impact of mutations identified in several ribosome protein genes in Diamond-Blackfan anemia, a disease that affects red blood cell formation. This work, performed through several collaborations, was supported by ANR, NIH, FRM, ARC as well as the French patient association AFMBD (www.afmbd.org).

  • The Cajal Body localisation signal of box C/D scaRNAs finally identified

    While the Cajal Body targeting element of human box H/ACA scaRNAs (the CAB box) was determined in 2003 by the group led by Tamas Kiss at the LBME, the Cajal Body localization signal for the box C/D scaRNAs remained up-to-now unidentified. However, thanks to the newly identified box C/D scaRNA mgU2-47, Tamas Kiss' group showed that GU-rich repeat RNA sequences compose the Cajal Body localization signal of box C/D scaRNAs in vertebrates.


  • TIP49 proteins : identification of the water-activating amino acid residues required for the associative mechanism of ATP hydrolysis.

    In collaboration with the Saint Petersburg State Polytechnical University and the University College of London, the team led by Emmanuel Käs and Mikhail Grigoriev of the LBME (Toulouse, France) highlighted a particular structural organization of the ATP hydrolysis pockets of the TIP49 proteins and by mutational analysis explained the mechanisms of their weak but essential ATPase activity.


  • Chromatin immunoprecipitation indirect peaks highlight long-range interactions of insulator proteins and Pol II pausing

    The group led by Olivier Cuvier from the LBME (Toulouse, France), have recently developed a new predictional strategy for long-range interactions between regulating factors and their remote target genes. This study, published in Molecular Cell, shows that these contacts, made possible via chromatin loops, are frequently involved in the regulation of distant genes. This method opens great opportunities for the understanding of complex networks of gene regulation.


  • Ancestral organization of HMG-Box factors involved in ribosomal DNA transcription

    The group "Dynamic Nuclear Organization" of the LBME in collaboration with Dr. Brian McStay (NUI Galway, Ireland) have unveiled an ancestral organization of HMG-Box factors involved in ribosomal DNA transcription from yeast to human. UBF1 in human and Hmo1 in budding yeast have related functions in vivo.


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  • Chromosomes dynamics revealed by biophysics

    Development of new techniques of optical microscopy was used to examine the movement and folding of chromosomes within living cells. This work published in Genome Research and the Journal of Cell Biology unveiled the biophysical properties of chromosomes, thus explaining their organizing principle. It was conducted by biologists and physicists from the Laboratoire de biologie moléculaire eucaryote (CNRS/Université Toulouse III – Paul Sabatier), the Laboratoire d'analyse et d'architecture des systèmes (CNRS) and the Laboratoire de physique théorique de la matière condensée (CNRS/UPMC), in collaboration with the Pasteur Institute and the Indian Council of scientific and Industrial Research. Five of the teams involved in this work are part of the research group "Nuclear Architecture and Dynamics" of the CNRS.

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  • Yeast chromosome structure

    The group "Dynamic Nuclear Organization" of the LBME, in collaboration with Dr. Aurélien Bancaud (LAAS, Toulouse, France) and Dr Purnima Bhargava (CCMB, Hyderabad, India), have investigated the conformation and dynamics of budding yeast chromosomes. Using high-throughput live cell microscopy, they have characterized the conformation and dynamics of the longest chromosome of S. cerevisiae.


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  • TFIIH and ribosome biogenesis

    In collaboration with Dr Giglia-Mari (IPBS, Toulouse, France), researchers from the LBME could better define TFIIH function in RNA polymerase I transcription and ribosome maturation. Their findings provide evidence that defective ribosome synthesis represents a new faulty mechanism involved in the pathophysiology of TFIIH-related diseases.


  • Osmotic stress and genome organisation

    Researchers from the LBME (Toulouse, France), in collaboration with Dr. Eulalia Nadal and Francesc Posas (from the university Pompeu Fabra in Barcelona, Spain) have shown the role of the kinase Hog1 in the organization of the yeast genome during osmotic stress.


  • Old drug, new target

    The ellipticine family contains a number of potent anticancer therapeutic agents, some having progressed to stage I and II clinical trials; however, the mechanism by which many of the compounds work remains unclear. Kostya Panov's team (Belfast, Ireland), in collaboration with researchers from the LBME showed that a number of the ellipticines, including 9-hydroxyellipticine, are potent and specific inhibitors of RNA polymerase I transcription.


  • Chromatin structure and gene looping regulate expression of the Cyclin D1 gene in breast cancer cells.

    We demonstrate that release of intragenic chromatin looping is required for rapid transcription activation in response to stimuli, in particular estrogen.


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  • RNA elements directing the assembly of the 7SK 'core' RNP

    Researchers from the LBME (Toulouse, France) have determined the sequence and structural elements of human 7SK snRNA directing assembly of the 7SK 'core' snRNP, that coordinates specific recruitment and inhibition of the general Pol II transcription elongation factor, P-TEFb. This work has been reported in Nucleic Acids Research in March 2013.


  • Microprocessor dynamics and interactions at endogenous imprinted C19MC microRNA genes

    Researchers from the LBME (Toulouse, France), the IGMM (Montpellier, France) and the Aarhus University (Denmark) have recently developed a cell imaging approach that enables the visualization of microRNA biogenesis in living human cells and at the level of a single microRNA cluster. Their work is described in details in an article of the Journal of Cell Science.

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  • Ser7 Phosphorylation of the CTD Recruits the RPAP2 Ser5 Phosphatase to snRNA Genes

    Researchers from the LBME and from the University of Oxford have recently demonstrated that phosphorylation of Serine 7 within the RNA polymerase II carboxyl-terminal domain (CTD) initiates a cascade of events critical for proper small nuclear RNA (snRNA) genes expression. This mechanism has been described in Mol Cell. 2012 Jan 13;45(1):111-22. Epub 2011 Dec 1.

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Laboratoire de Biologie
Moléculaire Eucaryote
UMR 5099