Reversible Membrane Tethering by ZipA Determines FtsZ Polymerization in Two and Three Dimensions

In most bacteria, the early step of septum formation implies the association of soluble FtsZ polymers with the cytoplasmic membrane. ZipA, together with FtsA, provides membrane tethering to FtsZ in Escherichia coli, forming a dynamic proto-ring that serves as an assembly scaffold for the remaining elements of the divisome. Despite their importance for bacterial cell division, multivalent interactions between proto-ring elements at membrane surfaces remain poorly characterized in quantitative terms. We measured the binding of FtsZ to ZipA incorporated in supported lipid bilayers at controlled densities by using a combination of biophysical surface-sensitive techniques (quartz crystal microbalance and spectroscopic ellipsometry) and analyzed how ZipA density and FtsZ concentration control the state of assembly of FtsZ. We found that ZipA attachment enables FtsZ-GMPCPP (where GMPCPP is a GTP analogue with a reduced level of hydrolysis) to assemble in several distinct ways: (i) two-dimensional polymerization at the membrane and (ii) three-dimensional polymerization from the membrane into the solution phase where this may be associated with the formation of higher-order complexes. In these processes, ZipA is required to enrich FtsZ at the surface but the FtsZ bulk concentration defines which morphology is being formed. Moreover, we report a strong effect of the nucleotide (GDP vs GMPCPP/GTP) on the kinetics of ZipA association/dissociation of FtsZ. These results provide insights into the mode of interaction of proto-ring elements in minimal membrane systems and contribute to the completion of our understanding of the initial events of bacterial division

The bacterial DNA binding protein matp involved in linking the nucleoid terminal domain to the divisome at midcell interacts with lipid membranes

© 2019 Monterroso et al. Division ring formation at midcell is controlled by various mechanisms in Escherichia coli, one of them being the linkage between the chromosomal Ter macrodomain and the Z-ring mediated by MatP, a DNA binding protein that organizes this macrodomain and contributes to the prevention of premature chromosome segregation. Here we show that, during cell division, just before splitting the daughter cells, MatP seems to localize close to the cytoplasmic membrane, suggesting that this protein might interact with lipids. To test this hypothesis, we investigated MatP interaction with lipids in vitro. We found that, when encapsulated inside vesicles and microdroplets generated by microfluidics, MatP accumulates at phospholipid bilayers and monolayers matching the lipid composition in the E. coli inner membrane. MatP binding to lipids was independently confirmed using lipid-coated microbeads and biolayer interferometry assays, which suggested that the recognition is mainly hydrophobic. Interaction of MatP with the lipid membranes also occurs in the presence of the DNA sequences specifically targeted by the protein, but there is no evidence of ternary membrane/protein/DNA complexes. We propose that the association of MatP with lipids may modulate its spatiotemporal localization and its recognition of other ligands. IMPORTANCE The division of an E. coli cell into two daughter cells with equal genomic information and similar size requires duplication and segregation of the chromosome and subsequent scission of the envelope by a protein ring, the Z-ring. MatP is a DNA binding protein that contributes both to the positioning of the Z-ring at midcell and the temporal control of nucleoid segregation. Our integrated in vivo and in vitro analysis provides evidence that MatP can interact with lipid membranes reproducing the phospholipid mixture in the E. coli inner membrane, without concomitant recruitment of the short DNA sequences specifically targeted by MatP. This observation strongly suggests that the membrane may play a role in the regulation of the function and localization of MatP, which could be relevant for the coordination of the two fundamental processes in which this protein participates, nucleoid segregation and cell division

MADCOVID-CSIC: Research and design of scientific dissemination activities on COVID-19 aimed at the Spanish youth

MADCOVID-CSIC is an outreach project aimed at young people concentrating on the most interesting aspects about the pandemic. These ranged from contagion to emotional impact. It is financed by the Recovery Fund and belongs to the Social Forum of the PTI+ Global Health.Objectives: • Disseminate, inform and promote knowledge about the pandemic among young people. • Promote greater awareness of young people about the risks of COVID-19. • Encourage young people to be the link of information and dissemination with their immediate family and friends. • Help young people emotionally manage the pandemic.Methods: First we sent a questionnaire to the teacher in order to determine the topics that interest the most: disease,contagion, vaccine, duration of the pandemic, misinformation, fake news and emotional management. The content of the talks is adapted to priorities. Then, an assessment of the experience is made between speakers and teachers to detect changes in behavior and perception of the pandemic among the students.Results and conclusions: To date, more than 25 talks have been given in educational centers, 11 of them in collaboration with secondary schools associated with the CSIC’s Science dissemination Project “Ciencia en el Barrio”, orientated to socially and vulnerable neighborhood in Madrid and the surrounded metropolitan area. In the talks, emotional management is treated preferentially, through collaboration with a cabinet of psychologists that is receiving great interest from teachers and students. They learn to recognize and name emotions, normalizing them and discarding emotional garbage, favoring more emotionally proactive, tolerant and healthy attitudes.Peer reviewe