Unite and Unrule! Reflections of a co-created pedagogy for transformation

Reader notes • As a collective, we experimented with co-creation as means to develop a more creative, innovative and collaborative space in order to inspire (in)direct transformations in the larger HE system we study and work in. • Our approach to co-creation, as a specific form of collaboration, is inspired by insights from critical, contemplative, social justice and relational pedagogy based on design principles derived from regenerative development. • In this case study, we highlight two interrelated features of our co-creation approach to developing transgressive learning spaces: 1) relational learning beyond individualism, and 2) from competition towards reflective and self-directed learning

Unite and Unrule! Reflections of a co-created pedagogy for transformation

Reader notes • As a collective, we experimented with co-creation as means to develop a more creative, innovative and collaborative space in order to inspire (in)direct transformations in the larger HE system we study and work in. • Our approach to co-creation, as a specific form of collaboration, is inspired by insights from critical, contemplative, social justice and relational pedagogy based on design principles derived from regenerative development. • In this case study, we highlight two interrelated features of our co-creation approach to developing transgressive learning spaces: 1) relational learning beyond individualism, and 2) from competition towards reflective and self-directed learning

Outer membrane protein folding from an energy landscape perspective

The cell envelope is essential for the survival of Gram-negative bacteria. This specialised membrane is densely packed with outer membrane proteins (OMPs), which perform a variety of functions. How OMPs fold into this crowded environment remains an open question. Here, we review current knowledge about OFMP folding mechanisms in vitro and discuss how the need to fold to a stable native state has shaped their folding energy landscapes. We also highlight the role of chaperones and the β-barrel assembly machinery (BAM) in assisting OMP folding in vivo and discuss proposed mechanisms by which this fascinating machinery may catalyse OMP folding

Factors Defining the Functional Oligomeric State of Escherichia coli DegP Protease

Escherichia coli DegP protein is a periplasmic protein that functions both as a protease and as a chaperone. In the absence of substrate, DegP oligomerizes as a hexameric cage but in its presence DegP reorganizes into 12 and 24-mer cages with large chambers that house the substrate for degradation or refolding. Here, we studied the factors that determine the oligomeric state adopted by DegP in the presence of substrate. Using size exclusion chromatography and electron microscopy, we found that the size of the substrate molecule is the main factor conditioning the oligomeric state adopted by the enzyme. Other factors such as temperature, a major regulatory factor of the activity of this enzyme, did not influence the oligomeric state adopted by DegP. In addition, we observed that substrate concentration exerted an effect only when large substrates (full-length proteins) were used. However, small substrate molecules (peptides) always triggered the same oligomeric state regardless of their concentration. These results clarify important aspects of the regulation of the oligomeric state of DegP

Involvement of N-acetylmuramyl-L-alanine amidases in cell separation and antibiotic-induced autolysis of Escherichia coli

N-acetylmuramyl-L-alanine amidases are widely distributed among bacteria. However, in Escherichia coli, only one periplasmic amidase has been described until now, which is suggested to play a role in murein recycling. Here, we report that three amidases, named AmiA, B and C, exist in E. coli and that they are involved in splitting of the murein septum during cell division. Moreover, the amidases were shown to act as powerful autolytic enzymes in the presence of antibiotics. Deletion mutants in amiA, B and C were growing in long chains of unseparated cells and displayed a tolerant response to the normally lytic combination of aztreonam and bulgecin. Isolated murein sacculi of these chain-forming mutants showed rings of thickened murein at the site of blocked septation. In vitro, these murein ring structures were digested more slowly by muramidases than the surrounding murein. In contrast, when treated with the amidase AmiC or the endopeptidase MepA, the rings disappeared, and gaps developed at these sites in the murein sacculi. These results are taken as evidence that highly stressed murein cross-bridges are concentrated at the site of blocked cell division, which, when cleaved, result in cracking of the sacculus at this site. As amidase deletion mutants accumulate trimeric and tetrameric cross-links in their murein, it is suggested that these structures mark the division site before cleavage of the septum

Unite and Unrule! Reflections of a co-created pedagogy for transformation

Reader notes • As a collective, we experimented with co-creation as means to develop a more creative, innovative and collaborative space in order to inspire (in)direct transformations in the larger HE system we study and work in. • Our approach to co-creation, as a specific form of collaboration, is inspired by insights from critical, contemplative, social justice and relational pedagogy based on design principles derived from regenerative development. • In this case study, we highlight two interrelated features of our co-creation approach to developing transgressive learning spaces: 1) relational learning beyond individualism, and 2) from competition towards reflective and self-directed learning