Transposons of the Tn 3 family form a widespread and remarkably homogeneous group of bacterial transposable elements in terms of transposition functions and an extremely versatile system for mediating gene reassortment and genomic plasticity owing to their modular organization. They have made major contributions to antimicrobial drug resistance dissemination or to endowing environmental bacteria with novel catabolic capacities. Here, we discuss the dynamic aspects inherent to the diversity and mosaic structure of Tn 3 -family transposons and their derivatives. We also provide an overview of current knowledge of the replicative transposition mechanism of the family, emphasizing most recent work aimed at understanding this mechanism at the biochemical level. Previous and recent data are put in perspective with those obtained for other transposable elements to build up a tentative model linking the activities of the Tn 3 -family transposase protein with the cellular process of DNA replication, suggesting new lines for further investigation. Finally, we summarize our current view of the DNA site-specific recombination mechanisms responsible for converting replicative transposition intermediates into final products, comparing paradigm systems using a serine recombinase with more recently characterized systems that use a tyrosine recombinase.

HOX proteins define a family of key transcription factors regulating animal embryogenesis. HOX genes have also been linked to oncogenesis and HOXA1 has been described to be active in several cancers, including breast cancer. Through a proteome-wide interaction screening, we previously identified the TNFR-associated proteins RBCK1/HOIL-1 and TRAF2 as HOXA1 interactors suggesting that HOXA1 is functionally linked to the TNF/NF-κB signaling pathway. Here, we reveal a strong positive correlation between expression of HOXA1 and of members of the TNF/NF-κB pathway in breast tumor datasets. Functionally, we demonstrate that HOXA1 can activate NF-κB and operates upstream of the NF-κB inhibitor IκB. Consistently, we next demonstrate that the HOXA1-mediated activation of NF-κB is non-transcriptional and that RBCK1 and TRAF2 influences on NF-κB are epistatic to HOXA1. We also identify an 11 Histidine repeat and the homeodomain of HOXA1 to be required both for RBCK1 and TRAF2 interaction and NF-κB stimulation. Finally, we highlight that activation of NF-κB is crucial for HOXA1 oncogenic activity.

In a permanent quest for profit, employees can be reduced to a mere function or instrument, dissociated from their quality as individuals for the organization's ends. Experiencing such a feeling as an employee has been called organizational dehumanization. Scholars have recently suggested that organizational dehumanization may play a key role in the development of emotional labor. However, how organizational dehumanization and two main emotional labor strategies (i.e., surface and deep acting) are causally related remains unclear in this literature. In the present research, we argue that employees who experience organizational dehumanization and whose self is thus threatened then engage in surface acting to "conserve" their self or in deep acting to "give up" their self in service of the role. Overall, the combined results of three studies offer strong evidence that organizational dehumanization leads employees to perform more surface acting, but not more deep acting. Unexpectedly, our findings also indicate that deep acting reduces the perception of being dehumanized by the organization. In showing this, the present research sheds light on the potential dark side of deep acting, by suggesting that this strategy can change employees' perspectives in a way that may encourage them to stay in an organization that treats them as a means to an end. (PsycInfo Database Record (c) 2021 APA, all rights reserved).