Two dynamin-like proteins stabilize FtsZ rings during Streptomyces sporulation

Research output: Contribution to journalArticle


title = "Two dynamin-like proteins stabilize FtsZ rings during Streptomyces sporulation",
abstract = "During sporulation, the filamentous bacteria Streptomyces undergo a massive cell division event in which the synthesis of ladders of sporulation septa convert multigenomic hyphae into chains of unigenomic spores. This process requires cytokinetic Z-rings formed by the bacterial tubulin homolog FtsZ, and the stabilization of the newly formed Z-rings is crucial for completion of septum synthesis. Here we show that two dynamin-like proteins, DynA and DynB, play critical roles in this process. Dynamins are a family of large, multidomain GTPases involved in key cellular processes in eukaryotes, including vesicle trafficking and organelle division. Many bacterial genomes encode dynamin-like proteins, but the biological function of these proteins has remained largely enigmatic. Using a cell biological approach, we show that the two Streptomyces dynamins specifically localize to sporulation septa in an FtsZ-dependent manner. Moreover, dynamin mutants have a cell division defect due to the decreased stability of sporulation-specific Z-rings, as demonstrated by kymographs derived from time-lapse images of FtsZ ladder formation. This defect causes the premature disassembly of individual Z-rings, leading to the frequent abortion of septum synthesis, which in turn results in the production of long spore-like compartments with multiple chromosomes. Two-hybrid analysis revealed that the dynamins are part of the cell division machinery and that they mediate their effects on Z-ring stability during developmentally controlled cell division via a network of protein–protein interactions involving DynA, DynB, FtsZ, SepF, SepF2, and the FtsZ-positioning protein SsgB.",
keywords = "Bacterial dynamins, Cell division, FtsZ, Sporulation, Streptomyces",
author = "Susan Schlimpert and Sebastian Wasserstrom and Govind Chandra and Bibb, {Maureen J.} and Findlay, {Kim C.} and Klas Fl{\"a}rdh and Buttner, {Mark J.}",
year = "2017",
month = "7",
day = "25",
doi = "10.1073/pnas.1704612114",
language = "English",
volume = "114",
pages = "E6176--E6183",
journal = "Proceedings of the National Academy of Sciences",
issn = "1091-6490",
publisher = "National Acad Sciences",
number = "30",