Pharmacological modulation of the ER stress response ameliorates oculopharyngeal muscular dystrophy

International audienc

Agir sur le travail des managers : des enjeux de métier pour les ergonomes, pour les managers

Managers’ work and management issues are nowadays a major concern for ergonomist practitioners and researchers. In this paper, we highlight societal and corporate evolutions and the way that ergonomics has evolved as a result. We propose a reading of the evolution that has been affecting companies for the last forty years, and show how the tertiarization and financialization of the economy and of companies have led them to deploy more rigid forms of organization that accentuate the control and demands of customers. We go on to observe that this evolution has not been uniform consistent, because the 1990s were the cradle of attempts to add to the tasks of operators by delegating tasks from middle management, while at the same time highlighting the fact that managers’ jobs have been transformed, particularly by a move away from actual workof attempts to enrich the tasks of operators by delegating tasks to middle management, while pointing out that. But gradually, the work of managers was transformed, particularly by moving away from work (Gomez, 2013). We then make the observation that in response to these developments, ergonomists have looked at different levels of organizational determinants, in order to improve the sustainability of the effects and to continue the work already carried out on business development of the activity. Finally, we defend the utility of developing ergonomic approaches to managers’ work, both for its key role in organizational functioning, particularly regarding regulations, and for the role it plays in the development of the activity of other employees. Hence today, more than ever, their work becomes an essential object of study and above all a major target for organizational intervention. We will see that current and future societal transitions reinforce this position

Le Néolithique final de Payennet à Gardanne (Bouches-du-Rhône)

International audienceC’est un projet d’aménagement routier comprenant une mise en deux fois deux voies de la RD6 et la construction d’échangeurs qui a permis la découverte de structures du Néolithique final au lieu-dit Payennet et dans ses environs

Specific interactions between HIV-1 nucleocapsid protein and the TAR element.

During retroviral reverse transcription, the minus-strand strong-stop DNA (ss-cDNA) is transferred to the 3' end of the genomic RNA and this requires the repeat (R) sequences present at both ends of the genome. In vitro, the human immunodeficiency virus type 1 (HIV-1) R sequence can promote DNA strand transfer when present in ectopic internal positions. Using HIV-1 model systems, the R sequences and nucleocapsid protein (NC) were found to be key determinants of ss-cDNA transfer. To gain insights into specific interactions between HIV-1 NC and RNA and the influence of NC on R folding, we investigated the secondary structures of R in two natural contexts, namely at the 5' or 3' end of RNAs representing the terminal regions of the genome, and in two ectopic internal positions that also support efficient minus-strand transfer. To investigate the roles of NC zinc fingers and flanking basic domains in the NC/RNA interactions, we used NC mutants. Analyses of the viral RNA/NC complexes by chemical and enzymatic probings, and gel retardation assays were performed under conditions allowing ss-cDNA transfer by reverse transcriptase. We report that NC binds the TAR apical loop specifically in the four genetic contexts without changing the folding of the TAR hairpin and R region significantly, and this requires the NC zinc fingers. In addition, we show that efficient annealing of cTAR DNA to the 3' R relies on sequence complementarities between TAR and cTAR terminal loops. These findings suggest that the TAR apical loop in the acceptor RNA is the initiation site for the annealing reaction that is chaperoned by NC during the minus-strand transfer

Buffering deleterious polymorphisms in highly constrained parts of HIV-1 envelope by flexible regions

International audienceAbstractBackgroundCovariation is an essential process that leads to coevolution of parts of proteins and genomes. In organisms subject to strong selective pressure, coevolution is central to keep the balance between the opposite requirements of antigenic variation and retention of functionality. Being the viral component most exposed to the external environment, the HIV-1 glycoprotein gp120 constitutes the main target of the immune response. Accordingly its more external portions are characterised by extensive sequence heterogeneity fostering constant antigenic variation.ResultsWe report that a single polymorphism, present at the level of the viral population in the conserved internal region C2, was sufficient to totally abolish Env functionality when introduced in an exogenous genetic context. The prominent defect of the non-functional protein is a block occurring after recognition of the co-receptor CCR5, likely due to an interference with the subsequent conformational changes that lead to membrane fusion. We also report that the presence of compensatory polymorphisms at the level of the external and hypervariable region V3 fully restored the functionality of the protein. The functional revertant presents different antigenic profiles and sensitivity to the entry inhibitor TAK 779.ConclusionsOur data suggest that variable regions, besides harbouring intrinsic extensive antigenic diversity, can also contribute to sequence diversification in more structurally constrained parts of the gp120 by buffering the deleterious effect of polymorphisms, further increasing the genetic flexibility of the protein and the antigenic repertoire of the viral population

Comprehension et methodes de prevention pour limiter les lesions musculo-squelettiques lies aux gestes repetitifs dans une entreprise de la plasturgie

Available from INIST (FR), Document Supply Service, under shelf-number : AR 16550 / INIST-CNRS - Institut de l'Information Scientifique et TechniqueSIGLEMinistere de l'Education Nationale de l'Enseignement Superieur et de la Recherche, 75 - Paris (France)FRFranc