[Effort-Reward Imbalance, Ability to Work and the Desire for Career Exits: a Cross-sectional Study of Nurses]. / Gratifikationskrisen, Arbeitsfähigkeit und Wunsch nach beruflichen Veränderungen ­ eine Querschnittsstudie bei Pflegepersonen.

INTRODUCTION: Since the Sars-Cov-2 pandemic, the working conditions of professional caregivers have tougher. This has lead to an increased desire to leave the profession. Since thoughts of leaving are influenced by factors such as ability to work and the relationship between effort and reward, both should be recorded and examined in relation to the desire to leave the profession. METHODOLOGY: In a standardized, online-based cross-sectional study, nurses from all areas were asked about their ability to work (Work Ability Index: WAI), the ratio of effort and reward (Effort-Reward-Imbalance: ERI-Ratio) as well as their desire to either leave the job or to change employers. RESULTS: A total of 2,689 questionnaires returned by nurses (average 41.3 years old, 75.1% female) were evaluated. The WAI indicates an average working ability (37.9 (6.7)). Nurses put in more effort than they get rewarded for (ERI ratio 1.7 (0.5)). 38.3% of the nurses considered leaving their job several times a month or more frequently, 30.6% to change their employers. Predicting factors were WAI (OR 0.881, 95%-CI 0.866; 0.897 and 0.923, 95%-CI 0.908; 0.938) and ERI ratio (OR 4.076, 95%-CI 3.224; 5.149 and 4.203, 95%-CI 3.312; 5.334). CONCLUSION: The ability to work and, in particular, the perception of professional effort and the reward received becomes apparent as having an influence on the idea of leaving the profession. The present results show that the ERI is of particular importance. Accordingly, it is important to find out which reward factors have a positive effect on remaining in the profession. The proportion of nurses with an academic degree is higher than expected which might have influenced the results.

ParB-type DNA Segregation Proteins Are CTP-Dependent Molecular Switches.

During cell division, newly replicated DNA is actively segregated to the daughter cells. In most bacteria, this process involves the DNA-binding protein ParB, which condenses the centromeric regions of sister DNA molecules into kinetochore-like structures that recruit the DNA partition ATPase ParA and the prokaroytic SMC/condensin complex. Here, we report the crystal structure of a ParB-like protein (PadC) that emerges to tightly bind the ribonucleotide CTP. The CTP-binding pocket of PadC is conserved in ParB and composed of signature motifs known to be essential for ParB function. We find that ParB indeed interacts with CTP and requires nucleotide binding for DNA condensation in vivo. We further show that CTP-binding modulates the affinity of ParB for centromeric parS sites, whereas parS recognition stimulates its CTPase activity. ParB proteins thus emerge as a new class of CTP-dependent molecular switches that act in concert with ATPases and GTPases to control fundamental cellular functions.