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Short FtsZ filaments can drive asymmetric cell envelope constriction at the onset of bacterial cytokinesis
Author(s) -
Yao Qing,
Jewett Andrew I,
Chang YiWei,
Oikonomou Catherine M,
Beeby Morgan,
Iancu Cristina V,
Briegel Ariane,
Ghosal Debnath,
Jensen Grant J
Publication year - 2017
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.15252/embj.201696235
Subject(s) - ftsz , caulobacter crescentus , cytokinesis , peptidoglycan , biology , cell division , mreb , cytoskeleton , microbiology and biotechnology , cell envelope , cytoplasm , tubulin , bacterial cell structure , cell , cell wall , microtubule , genetics , bacteria , cell cycle , escherichia coli , gene
FtsZ, the bacterial homologue of eukaryotic tubulin, plays a central role in cell division in nearly all bacteria and many archaea. It forms filaments under the cytoplasmic membrane at the division site where, together with other proteins it recruits, it drives peptidoglycan synthesis and constricts the cell. Despite extensive study, the arrangement of FtsZ filaments and their role in division continue to be debated. Here, we apply electron cryotomography to image the native structure of intact dividing cells and show that constriction in a variety of Gram‐negative bacterial cells, including Proteus mirabilis and Caulobacter crescentus , initiates asymmetrically, accompanied by asymmetric peptidoglycan incorporation and short FtsZ‐like filament formation. These results show that a complete ring of FtsZ is not required for constriction and lead us to propose a model for FtsZ‐driven division in which short dynamic FtsZ filaments can drive initial peptidoglycan synthesis and envelope constriction at the onset of cytokinesis, later increasing in length and number to encircle the division plane and complete constriction.