{"title":"Tubules, Rods, and Spirals: Diverse Modes of SepF-FtsZ Assembling","authors":"Jagrity Choudhury, Barnali N. Chaudhuri","doi":"10.1002/cm.21975","DOIUrl":null,"url":null,"abstract":"<div>\n \n <p>Z-ring formation by FtsZ, the master assembler of the divisome, is a key step in bacterial cell division. Membrane anchoring of the Z-ring requires the assistance of dedicated Z-ring binding proteins, such as SepF and FtsA. SepF participates in bundling and membrane anchoring of FtsZ in gram-positive bacteria. We report in vitro biophysical studies of the interactions between FtsZ and a cytoplasmic component of cognate SepF from three different bacteria: <i>Mycobacterium tuberculosis</i>, <i>Staphylococcus aureus</i>, and <i>Enterococcus gallinarum.</i> While the cytosolic domain of SepF from <i>M. tuberculosis</i> is primarily a dimer, those from <i>S. aureus</i> and <i>E. gallinarum</i> polymerize to form ring-like structures. Mycobacterial SepF helps in the bundling of FtsZ filaments to form thick filaments and large spirals. On the other hand, ring-forming SepF from the <i>Firmicutes</i> bundle FtsZ into tubules. Our results suggest that the oligomeric form of SepF directs how it bundles FtsZ filaments.</p>\n </div>","PeriodicalId":55186,"journal":{"name":"Cytoskeleton","volume":"82 7","pages":"432-443"},"PeriodicalIF":1.6000,"publicationDate":"2024-12-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Cytoskeleton","FirstCategoryId":"99","ListUrlMain":"https://onlinelibrary.wiley.com/doi/10.1002/cm.21975","RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q4","JCRName":"CELL BIOLOGY","Score":null,"Total":0}
引用次数: 0
Abstract
Z-ring formation by FtsZ, the master assembler of the divisome, is a key step in bacterial cell division. Membrane anchoring of the Z-ring requires the assistance of dedicated Z-ring binding proteins, such as SepF and FtsA. SepF participates in bundling and membrane anchoring of FtsZ in gram-positive bacteria. We report in vitro biophysical studies of the interactions between FtsZ and a cytoplasmic component of cognate SepF from three different bacteria: Mycobacterium tuberculosis, Staphylococcus aureus, and Enterococcus gallinarum. While the cytosolic domain of SepF from M. tuberculosis is primarily a dimer, those from S. aureus and E. gallinarum polymerize to form ring-like structures. Mycobacterial SepF helps in the bundling of FtsZ filaments to form thick filaments and large spirals. On the other hand, ring-forming SepF from the Firmicutes bundle FtsZ into tubules. Our results suggest that the oligomeric form of SepF directs how it bundles FtsZ filaments.
期刊介绍:
Cytoskeleton focuses on all aspects of cytoskeletal research in healthy and diseased states, spanning genetic and cell biological observations, biochemical, biophysical and structural studies, mathematical modeling and theory. This includes, but is certainly not limited to, classic polymer systems of eukaryotic cells and their structural sites of attachment on membranes and organelles, as well as the bacterial cytoskeleton, the nucleoskeleton, and uncoventional polymer systems with structural/organizational roles. Cytoskeleton is published in 12 issues annually, and special issues will be dedicated to especially-active or newly-emerging areas of cytoskeletal research.