VLTI-MATISSE L- and N-band aperture-synthesis imaging of the unclassified B[e] star FS Canis Majoris★

This is the final version. Available from EDP Sciences via the DOI in this record. Context. FS Canis Majoris (FS CMa, HD 45677) is an unclassified B[e] star surrounded by an inclined dust disk. The evolutionary stage of FS CMa is still debated. Perpendicular to the circumstellar disk, a bipolar outflow was detected. Infrared aperture-synthesis imaging provides us with a unique opportunity to study the disk structure. Aims. Our aim is to study the intensity distribution of the disk of FS CMa in the mid-infrared L and N bands. Methods. We performed aperture-synthesis imaging of FS CMa with the MATISSE instrument (Multi AperTure mid-Infrared SpectroScopic Experiment) in the low spectral resolution mode to obtain images in the L and N bands. We computed radiative transfer models that reproduce the L- and N-band intensity distributions of the resolved disks. Results. We present L- and N-band aperture-synthesis images of FS CMa reconstructed in the wavelength bands of 3.4-3.8 and 8.6-9.0 μm. In the L-band image, the inner rim region of an inclined circumstellar disk and the central object can be seen with a spatial resolution of 2.7 milliarcsec (mas). An inner disk cavity with an angular diameter of ~6 × 12 mas is resolved. The L-band disk consists of a bright northwestern (NW) disk region and a much fainter southeastern (SE) region. The images suggest that we are looking at the bright inner wall of the NW disk rim, which is on the far side of the disk. In the N band, only the bright NW disk region is seen. In addition to deriving the inclination and the inner disk radius, fitting the reconstructed brightness distributions via radiative transfer modelling allows one to constrain the innermost disk structure, in particular the shape of theinner disk rim.Science and Technology Facilities CouncilAgence Nationale de la Recheche (ANR)Agencia Nacional de Investigación y Desarrollo (ANID)Agencia Nacional de Investigación y Desarrollo (ANID)European Research CouncilEuropean Research CouncilEuropean Research CouncilHungarian NKFIH OTKAEuropean Research CouncilUNAM PAPIIT project IACONACyT projectFAPESPFAPESPNOVA, the Netherlands Research School for Astronom

VLTI-MATISSE L- and N-band aperture-synthesis imaging of the unclassified B[e] star FS Canis Majoris

Stars and planetary system

MATISSE, the VLTI mid-infrared imaging spectro-interferometer

GalaxiesStars and planetary systemsInstrumentatio

Mid-infrared circumstellar emission of the long-period Cepheid l Carinae resolved with VLTI/MATISSE

Stars and planetary system

An Oscillating MinD Protein Determines the Cellular Positioning of the Motility Machinery in Archaea

MinD proteins are well studied in rod-shaped bacteria such as E. coli, where they display self-organized pole-to-pole oscillations that are important for correct positioning of the Z-ring at mid-cell for cell division. Archaea also encode proteins belonging to the MinD family, but their functions are unknown. MinD homologous proteins were found to be widespread in Euryarchaeota and form a sister group to the bacterial MinD family, distinct from the ParA and other related ATPase families. We aimed to identify the function of four archaeal MinD proteins in the model archaeon Haloferax volcanii. Deletion of the minD genes did not cause cell division or size defects, and the Z-ring was still correctly positioned. Instead, one of the deletions (ΔminD4) reduced swimming motility and hampered the correct formation of motility machinery at the cell poles. In ΔminD4 cells, there is reduced formation of the motility structure and chemosensory arrays, which are essential for signal transduction. In bacteria, several members of the ParA family can position the motility structure and chemosensory arrays via binding to a landmark protein, and consequently these proteins do not oscillate along the cell axis. However, GFP-MinD4 displayed pole-to-pole oscillation and formed polar patches or foci in H. volcanii. The MinD4 membrane-targeting sequence (MTS), homologous to the bacterial MinD MTS, was essential for the oscillation. Surprisingly, mutant MinD4 proteins failed to form polar patches. Thus, MinD4 from H. volcanii combines traits of different bacterial ParA/MinD proteins