{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Middlemiss S"],"funding":["RCUK | Biotechnology and Biological Sciences Research Council","Wellcome Trust","Biotechnology and Biological Sciences Research Council"],"pagination":["5411"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11208587"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["15(1)"],"pubmed_abstract":["Most rod-shaped bacteria elongate by inserting new cell wall material into the inner surface of the cell sidewall. This is performed by class A penicillin binding proteins (PBPs) and a highly conserved protein complex, the elongasome, which moves processively around the cell circumference and inserts long glycan strands that act as barrel-hoop-like reinforcing structures, thereby giving rise to a rod-shaped cell. However, it remains unclear how elongasome synthesis dynamics and termination events are regulated to determine the length of these critical cell-reinforcing structures. To address this, we developed a method to track individual elongasome complexes around the entire circumference of Bacillus subtilis cells for minutes-long periods using single-molecule fluorescence microscopy. We"],"journal":["Nature communications"],"pubmed_title":["Molecular motor tug-of-war regulates elongasome cell wall synthesis dynamics in Bacillus subtilis."],"pmcid":["PMC11208587"],"funding_grant_id":["BB/X001482/1","BB/X001512/1","BB/M011186/1","206670/Z/17/Z"],"pubmed_authors":["Roberts DM","McMahon A","Blandenet M","Edwards JM","Whitley KD","Strahl H","Grimshaw J","Blu T","Middlemiss S","Sun Z","Holden S"],"additional_accession":[]},"is_claimable":false,"name":"Molecular motor tug-of-war regulates elongasome cell wall synthesis dynamics in Bacillus subtilis.","description":"Most rod-shaped bacteria elongate by inserting new cell wall material into the inner surface of the cell sidewall. This is performed by class A penicillin binding proteins (PBPs) and a highly conserved protein complex, the elongasome, which moves processively around the cell circumference and inserts long glycan strands that act as barrel-hoop-like reinforcing structures, thereby giving rise to a rod-shaped cell. However, it remains unclear how elongasome synthesis dynamics and termination events are regulated to determine the length of these critical cell-reinforcing structures. To address this, we developed a method to track individual elongasome complexes around the entire circumference of Bacillus subtilis cells for minutes-long periods using single-molecule fluorescence microscopy. We","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Jun","modification":"2025-04-04T21:22:31.628Z","creation":"2025-04-04T21:22:31.628Z"},"accession":"S-EPMC11208587","cross_references":{"pubmed":["38926336"],"doi":["10.1038/s41467-024-49785-x"]}}