INDIFFERENCIE : DROIT DE L'HOMME ET UNION EUROPEENNE

Conférences de l’IREDIES / IREDIES Conference Paper n° 2 /2019La présente étude est le fruit d’un travail collectif réalisé par les étudiants de la promotion 2018-2019 du Master 2 « Droits de l’homme et Union européenne » de l’Ecole de droit de la Sorbonne (Paris 1). Ce diplôme – qui a l’intérêt de disposer d’un séminaire entièrement consacré à l’étude de la Charte des droits fondamentaux de l’Union européenne – a été le lieu de réflexion de cette recherche menée avec enthousiasme et professionnalisme par tous les étudiants. Les travaux doctrinaux sur ce texte novateur sont en général centrés sur la manière dont la Cour de justice de l’Union l’interprète et l’applique. Or, il ne s’agit là que de la face visible de l’iceberg contentieux. Dans ce contexte, il est apparu essentiel de s’interroger sur la manière dont les juridictions internes avaient apprivoisé ce texte moderne (au regard de la variété des droits qu’il consacre) et complexe (au regard de son champ d’application).Les étudiants se sont répartis en trois groupes afin d’étudier la manière dont les juridictions internes (Conseil constitutionnel, Conseil d’Etat et Cour de cassation), mais également le législateur, se sont emparés de ce texte.Les résultats de cette étude, où l’outil statistique a constitué un support cardinal, démontrent que si la Charte des droits fondamentaux est connue du pouvoir législatif et des « acteurs » judiciaires, il n’est pas encore devenu une référence incontournable du processus législatif et de l’argumentaire des juges. L’antériorité de la Convention de sauvegarde des droits et libertés fondamentales comme les spécificités du champ d’application de la Charte sont deux éléments explicatifs d’un tel état de fait.Ce travail, mené avec sérieux et rigueur, méritait d’être rendu public au sein de la collection des Working papers de l’IREDIES

Cyclops: New modular software suite for cryo-EM

,rain designed as a graphical front-cild that allows easy control and interaction with tasks and programs is a new computer grams for 3D reconstruction of biological complexes using cryo-electron microscopy. Cyclops' current plug-his are designed for automated particle picking and include two new algorithms, automated carbon masking and quaternion based rotation space sampling, which are also presented here. Additional plug-ins are in the pipeline. Cyclops allows straightforward organization and visualization of all data and tasks and allows both interactive and batch-wise processing. Furthermore, it was designed for straightforward implementation in grid architectures. As a front-end to a collection of programs it provides a common interface to these programs, thus enhancing the usability of the suite and the productivity Of the User. (c) 2006 Elsevier Inc. All rights reserved

Visualization by cryo-electron microscopy of genomic RNA that binds to the protein capsid inside bacteriophage MS2

The icosahedrally symmetrized structure of bacteriophage MS2 as determined by cryo-electron microscopy (EM) reveals the presence of genomic RNA that attaches to coat-protein dimers. Earlier X-ray diffraction studies revealed similar interactions between the unique operator hairpin of the MS2 genomic RNA and the coat-protein dimer. This observation leads us to conclude that not only the operator, but also many other RNA sequences in the genome of MS2, are able to bind to the coat-protein dimer. A substantial number of potential coat-protein-dimer binding sites are present in the genome of MS2 that can account for the observed RNA densities in the EM map. Moreover, it appears that these stem-loop structures are able to bind in a similar fashion to the coat protein dimer as the wild-type operator hairpin. The EM map also shows additional density between the potential operator-binding sites, linking the RNA stem-loops together to form an icosahedral network around the 3 and 5-fold axes. This RNA network is bound to the inside of the MS2 capsid and probably influences both capsid stability and formation, supporting the idea that capsid formation and RNA packaging are intimately linked to each other

Crystal structure of an empty capsid of turnip yellow mosaic virus

Empty capsids (artificial top component) of turnip yellow mosaic virus were co-crystallized with an encapsidation initiator RNA hairpin. No clear density was observed for the RNA, but there were clear differences in the conformation of a loop of the coat protein at the opening of the pentameric capsomer (formed by five A-subunits) protruding from the capsid, compared to the corresponding loop in the intact virus. Further differences were found at the N terminus of the A-subunit. These differences have implications for the mechanism of decapsidation of the virus, required for infection

Recycling of aborted ribosomal 50S subunit-nascent chain-tRNA complexes by the heat shock protein Hsp15

When heat shock prematurely dissociates a translating bacterial ribosome, its 50S subunit is prevented from reinitiating protein synthesis by tRNA covalently linked to the unfinished protein chain that remains threaded through the exit tunnel. Hsp15, a highly upregulated bacterial heat shock protein, reactivates such dead-end complexes. Here, we show with cryo-electron microscopy reconstructions and functional assays that Hsp15 translocates the tRNA moiety from the A site to the P site of stalled 50S subunits. By stabilizing the tRNA in the P site, Hsp15 indirectly frees up the A site, allowing a release factor to land there and cleave off the tRNA. Such a release factor must be stop codon independent, suggesting a possible role for a poorly characterized class of putative release factors that are upregulated by cellular stress, lack a codon recognition domain and are conserved in eukaryotes