A dynamic duo: Understanding the roles of FtsZ and FtsA for Escherichia coli cell division through in vitro approaches

Radler, Philipp; Loose, Martin

doi:10.1016/j.ejcb.2023.151380

Cited by 5 publications

(1 citation statement)

References 206 publications

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“…The C-terminal part of FtsZ consists of an intrinsically disordered linker of variable length, followed by a conserved C-terminal tail region, and another short variable region (Buske andLevin, 2012, Heucus et al, 2017). The C-terminal tail serves as an interaction site for many FtsZ interacting proteins, including those that anchor FtsZ to the membrane (Cameron and Margolin, 2024, Cendrowicz et al, 2012, Haney et al, 2001, Mosyak et al, 2000, Radler and Loose, 2024, Singh et al, 2007. FtsZ polymerize in a "head-to-tail" fashion, and the GTPase active site of FtsZ is formed at the inter-subunit interface of the polymer (Wagstaff et al, 2017).…”

Section: Introductionmentioning

confidence: 99%

Tubules, rods and spirals: diverse modes of SepF-FtsZ assembling

Choudhury,

Chaudhuri

2024

Preprint

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Z-ring formation by FtsZ, the master assembler of divisome, is a key step in bacterial cell division. Both formation and membrane anchoring of the Z-ring requires assistance of a number of Z-ring binding proteins, such as FtsA, EzrA, SepF, SepH and ZipA. 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 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 a dimer, those from S. aureus and E. gallinarum polymerize to form ring-like structures. Mycobacterial SepF helps in 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.

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Section: Introductionmentioning

confidence: 99%

Tubules, rods and spirals: diverse modes of SepF-FtsZ assembling

Choudhury,

Chaudhuri

2024

Preprint

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Editorial - In vitro reconstitution of cytoskeletal processes

Jégou,

Romet-Lemonne

2024

European Journal of Cell Biology

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O-glycosylation of intrinsically disordered regions regulates homeostasis of membrane proteins in streptococci

Rahman,

Zamakhaeva,

Rush

et al. 2024

Preprint

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Proteins harboring intrinsically disordered regions (IDRs) that lack regular secondary or tertiary structure are abundant across three domains of life. Here, using a deep neural network (DNN)-based method we predict IDRs in the extracytoplasmic proteome of Streptococcus mutans, Streptococcus pyogenes and Streptococcus pneumoniae. We identify a subset of the serine/threonine-rich IDRs and demonstrate that they are O-glycosylated with glucose by a GtrB-like glucosyltransferase in S. pyogenes and S. pneumoniae, and N-acetylgalactosamine by a Pgf-dependent mechanism in S. mutans. Loss of glycosylation leads to a defect in biofilm formation under ethanol-stressed conditions in S. mutans. We link this phenotype to a C-terminal IDR of peptidyl-prolyl isomerase PrsA which is protected from proteolytic degradation by O-glycosylation. The IDR length attenuates the efficiency of glycosylation and expression of PrsA. Taken together, our data support a model in which extracytoplasmic IDRs function as dynamic switches of protein homeostasis in streptococci.

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A dynamic duo: Understanding the roles of FtsZ and FtsA for Escherichia coli cell division through in vitro approaches

Cited by 5 publications

References 206 publications

Tubules, rods and spirals: diverse modes of SepF-FtsZ assembling

Tubules, rods and spirals: diverse modes of SepF-FtsZ assembling

Editorial - In vitro reconstitution of cytoskeletal processes

O-glycosylation of intrinsically disordered regions regulates homeostasis of membrane proteins in streptococci

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