[L'impossible quête des préposées aux bénéficiaires pour actualiser la bientraitance visée dans les politiques publiques du Québec.The impossible quest of health care aides to actualize the good treatment targeted in Quebec's public policies.]

Notre recherche visait à mettre en lumière les pratiques bientraitantes des préposées aux bénéficiaires en milieux d'hébergement pour aînés au Québec. L'objet de l'article est de faire ressortir la dichotomie entre les définitions de la bientraitance et son opérationnalisation. Dans la première partie, la notion de bientraitance dans le cadre de deux politiques gouvernementales québécoises est présentée. Ensuite, il est question du travail des préposées aux bénéficiaires en tant que vectrices de cette bientraitance dans la pratique. La troisième partie présente les résultats de notre recherche qui viennent soulever trois constats remettant en cause l'applicabilité des politiques publiques en cette matière : l'absence de reconnaissance d'un métier par définition bientraitant; les injonctions normatives à l'encontre du sens attribué à la bientraitance, et les obstacles organisationnels et sociopolitiques à la bientraitance. Ces constats sont réexaminés à la lumière des écrits dans la discussion, laquelle ouvre sur la notion de maltraitance organisationnelle.

Unique Structural Fold of LonBA Protease from Bacillus subtilis, a Member of a Newly Identified Subfamily of Lon Proteases.

ATP-dependent Lon proteases are key participants in the quality control system that supports the homeostasis of the cellular proteome. Based on their unique structural and biochemical properties, Lon proteases have been assigned in the MEROPS database to three subfamilies (A, B, and C). All Lons are single-chain, multidomain proteins containing an ATPase and protease domains, with different additional elements present in each subfamily. LonA and LonC proteases are soluble cytoplasmic enzymes, whereas LonBs are membrane-bound. Based on an analysis of the available sequences of Lon proteases, we identified a number of enzymes currently assigned to the LonB subfamily that, although presumably membrane-bound, include structural features more similar to their counterparts in the LonA subfamily. This observation was confirmed by the crystal structure of the proteolytic domain of the enzyme previously assigned as Bacillus subtilis LonB, combined with the modeled structure of its ATPase domain. Several structural features present in both domains differ from their counterparts in either LonA or LonB subfamilies. We thus postulate that this enzyme is the founding member of a newly identified LonBA subfamily, so far found only in the gene sequences of firmicutes.

'Good Treatment' in Residential Care Settings in Quebec: Meanings, Practices and Conditions.

The concept of 'bientraitance'(good treatment) of older adults was introduced in Quebec policy a few years prior to the pandemic, and its significance from the perspectives of those directly involved in care remains underexplored. Centring these perspectives, this article presents findings from a study of the meanings, practices and conditions of good treatment. Data was collected at three different residential care settings through world cafés with residents, staff, management, volunteers and family members (n = 61) and through interviews with care aides (n = 13). The study results indicate that those directly involved in care identify good treatment as fundamentally oriented towards developing and maintaining good relationships with residents; as contingent upon interpersonal, material, and organizational factors; and as requiring (more) time. Given the need for radical reform within Quebec's residential care settings revealed by the pandemic, it is imperative that these perspectives inform the changes introduced.

La participation sociale dans les résidences privées pour aînés.

Le vieillissement de la population invite à étudier les résidences privées pour aînés, notamment sous l'angle du lien social. Après leur emménagement en résidence, plusieurs aînés veulent continuer de participer activement à la société. Cette recherche qualitative exploratoire a pour objectif de mieux comprendre les perceptions et les expériences d'aînés vivant dans une résidence privée par rapport à leur participation sociale, sur le plan de leurs relations interpersonnelles et de leurs activités de loisirs. Onze entrevues individuelles ont été menées auprès de personnes vivant dans des résidences privées pour aînés de la région de la ville de Québec, au Canada. Sur le plan personnel, les facteurs centraux pour la participation sociale sont l'adaptation au nouveau milieu de vie, l'implication dans ce milieu, notamment par le biais du bénévolat, ainsi que l'état de santé de la personne. En ce qui concerne l'environnement social, les facteurs importants sont la proximité géographique de l'entourage, une offre variée d'activités et la stabilité du personnel. Au final, des recommandations sont formulées au sujet des stratégies d'intervention et des pistes de recherche, lesquelles donnent suite aux constats énoncés, et ce, afin de mieux soutenir la participation sociale en résidence privée pour aînés.

New insights into structural and functional relationships between LonA proteases and ClpB chaperones.

LonA proteases and ClpB chaperones are key components of the protein quality control system in bacterial cells. LonA proteases form a unique family of ATPases associated with diverse cellular activities (AAA+ ) proteins due to the presence of an unusual N-terminal region comprised of two domains: a ß-structured N domain and an α-helical domain, including the coiled-coil fragment, which is referred to as HI(CC). The arrangement of helices in the HI(CC) domain is reminiscent of the structure of the H1 domain of the first AAA+ module of ClpB chaperones. It has been hypothesized that LonA proteases with a single AAA+ module may also contain a part of another AAA+ module, the full version of which is present in ClpB. Here, we established and tested the structural basis of this hypothesis using the known crystal structures of various fragments of LonA proteases and ClpB chaperones, as well as the newly determined structure of the Escherichia coli LonA fragment (235-584). The similarities and differences in the corresponding domains of LonA proteases and ClpB chaperones were examined in structural terms. The results of our analysis, complemented by the finding of a singular match in the location of the most conserved axial pore-1 loop between the LonA NB domain and the NB2 domain of ClpB, support our hypothesis that there is a structural and functional relationship between two coiled-coil fragments and implies a similar mechanism of engagement of the pore-1 loops in the AAA+ modules of LonAs and ClpBs.

Limited proteolysis of E. coli ATP-dependent protease Lon - a unified view of the subunit architecture and characterization of isolated enzyme fragments.

We carried out chymotryptic digestion of multimeric ATP-dependent Lon protease from Escherichia coli. Four regions sensitive to proteolytic digestion were located in the enzyme and several fragments corresponding to the individual structural domains of the enzyme or their combinations were isolated. It was shown that (i) unlike the known AAA(+) proteins, the ATPase fragment (A) of Lon has no ATPase activity in spite of its ability to bind nucleotides, and it is monomeric in solution regardless of the presence of any effectors; (ii) the monomeric proteolytic domain (P) does not display proteolytic activity; (iii) in contrast to the inactive counterparts, the AP fragment is an oligomer and exhibits both the ATPase and proteolytic activities. However, unlike the full-length Lon, its AP fragment oligomerizes into a dimer or a tetramer only, exhibits the properties of a non-processive protease, and undergoes self-degradation upon ATP hydrolysis. These results reveal the crucial role played by the non-catalytic N fragment of Lon (including its coiled-coil region), as well as the contribution of individual domains to creation of the quaternary structure of the full-length enzyme, empowering its function as a processive protease.