DipM controls multiple autolysins and mediates a regulatory feedback loop promoting cell constriction in Caulobacter crescentus.

Proteins with a catalytically inactive LytM-type endopeptidase domain are important regulators of cell wall-degrading enzymes in bacteria. Here, we study their representative DipM, a factor promoting cell division in Caulobacter crescentus. We show that the LytM domain of DipM interacts with multiple autolysins, including the soluble lytic transglycosylases SdpA and SdpB, the amidase AmiC and the putative carboxypeptidase CrbA, and stimulates the activities of SdpA and AmiC.

Interacting bactofilins impact cell shape of the MreB-less multicellular Rhodomicrobium vannielii.

Most non-spherical bacteria rely on the actin-like MreB cytoskeleton to control synthesis of a cell-shaping and primarily rod-like cell wall. Diverging from simple rod shape generally requires accessory cytoskeletal elements, which locally interfere with the MreB-guided cell wall synthesis. Conserved and widespread representatives of this accessory cytoskeleton are bactofilins that polymerize into static, non-polar bundles of filaments.

Digitalization and disruptive change in rheumatology.

Introduction: Recently, many sectors have seen disruptive changes due to the rapid progress in information and communication technology (ICT). The aim of this systematic literature review was to develop a first understanding of what is known about new ICTs in rheumatology and their disruptive potential.

Methods: PubMed, LIVIVO, and EBSCO Discovery Service (EDS) databases were searched for relevant literature.