Structural Analysis of the Interaction between the Bacterial Cell Division Proteins FtsQ and FtsB

Kureisaite-Ciziene, Danguole; Varadajan, Aravindan; McLaughlin, Stephen H.; Glas, Marjolein; Silva, Alejandro Montón; Luirink, Rosa A.; Mueller, Carolin; Blaauwen, Tanneke den; Grossmann, Tom N.; Luirink, Joen; Löwe, Jan

doi:10.1128/mbio.01346-18

Cited by 42 publications

(75 citation statements)

References 43 publications

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“…S3). Consistently, the electron density map of FtsB N-terminus (residues 22–63) was not observed for FtsB in the crystal structure of FtsQB complex, which was reported recently by other group 26 . One possibility regarding the lack of electron density is that the membrane-proximal helix is disordered in the crystal of FtsQB complex; however, the crystal structure of the 30 juxta-membrane amino acids of FtsB showed that it forms a canonical coiled coil 27 , thus we excluded this possibility.…”

Section: Resultssupporting

confidence: 89%

Structural Insights into the FtsQ/FtsB/FtsL Complex, a Key Component of the Divisome

Choi

Kim

Yoon

et al. 2018

Sci Rep

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Bacterial cell division is a fundamental process that results in the physical separation of a mother cell into two daughter cells and involves a set of proteins known as the divisome. Among them, the FtsQ/FtsB/FtsL complex was known as a scaffold protein complex, but its overall structure and exact function is not precisely known. In this study, we have determined the crystal structure of the periplasmic domain of FtsQ in complex with the C-terminal fragment of FtsB, and showed that the C-terminal region of FtsB is a key binding region of FtsQ via mutational analysis in vitro and in vivo. We also obtained the solution structure of the periplasmic FtsQ/FtsB/FtsL complex by small angle X-ray scattering (SAXS), which reveals its structural organization. Interestingly, the SAXS and analytical gel filtration data showed that the FtsQ/FtsB/FtsL complex forms a 2:2:2 heterohexameric assembly in solution with the “Y” shape. Based on the model, the N-terminal directions of FtsQ and the FtsB/FtsL complex should be opposite, suggesting that the Y-shaped FtsQ/FtsB/FtsL complex might fit well into the curved membrane for membrane anchoring.

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Section: Resultssupporting

confidence: 89%

Structural Insights into the FtsQ/FtsB/FtsL Complex, a Key Component of the Divisome

Choi

Kim

Yoon

et al. 2018

Sci Rep

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“…TolB plays a role in OM invagination during cell constriction in the trans-envelope Tol-pal system (Zhuang et al, 2002;Gerding et al, 2007;Ridley and Lakey, 2015). The Fts opera, containing FtsA, FtsI, FtsL, and FtsQ, are involved in cell division (Chen and Beckwith, 2001;Kureisaite-Ciziene et al, 2018;Du et al, 2019). MrcA and MurA play a role in cell wall formation (Kock et al, 2004;Zhu et al, 2012), Tig is involved in protein export, and the only downregulated protein in the 11 proteins related to cell division (Martinez-Hackert and Hendrickson, 2009).…”

Section: Bioinformatics Analysis On the Cell Division And Cell Wall Bmentioning

confidence: 99%

Cyclic AMP-CRP Modulates the Cell Morphology of Klebsiella pneumoniae in High-Glucose Environment

Liu

et al. 2020

Front. Microbiol.

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Bacteria can modify their morphology in response to environmental stimuli for survival or host defense evasion. The rich glucose in vivo or in the Luria-Bertani (LB) medium shortened the cell length of Klebsiella pneumoniae. The environmental glucose decreased the levels of cyclic AMP (cAMP) and the transcription of crp, which declined the cAMP-cAMP receptor protein (cAMP-CRP) activity. The cell length of crp deletion mutant was significantly shorter than that of the wild type (0.981 ± 0.057 µm vs. 2.415 ± 0.075 µm, P < 0.001). These results indicated that the high environmental glucose alters the bacterial morphology to a round form through regulating the activity of cAMP-CRP complex. Comparative proteomics analysis showed increased expression of 10 proteins involved in cell division or cell wall biosynthesis in the crp deletion strain. Five of them (ompA, tolB, ybgC, ftsI, and rcsF) were selected to verify their expression in the high-glucose environment, and overexpression of tolB or rcsF shortened the bacterial length similar to that of the crp deletion strain. Electrophoretic mobility shift assay indicated that CRP directly negatively regulates the transcription of tolB and rcsF by binding to the promoter regions. This study first proved the role and partial regulation mechanism of CRP in altering cell morphology during infection and provided a theoretical basis for elucidating the mechanism in diabetes mellitus susceptible to K. pneumoniae.

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“…They also interact with FtsQ through their C-terminal domains that lie beyond the coiled-coil domains forming a 1:1:1 complex which may dimerize (13,15,18). Recently, a peptide corresponding to the C-terminal region of FtsB was crystallized bound to FtsQ (19,20).…”

Section: Introductionmentioning

confidence: 99%

Essential role for FtsL in activation of septal PG synthesis

Park

Lutkenhaus

2020

Preprint

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Spatiotemporal regulation of septal PG synthesis is achieved by coupling assembly and activation of the synthetic enzymes (FtsWI) to the Z ring, a cytoskeletal element required for division in most bacteria. In E. coli the recruitment of the FtsWI complex is dependent upon the cytoplasmic domain of FtsL, a component of the conserved FtsQLB complex. Once assembled, FtsWI is activated by the arrival of FtsN, which acts through FtsQLB and FtsA that are also essential for their recruitment. However, the mechanism of activation of FtsWI by FtsN is not clear. Here, we identify a region of FtsL that plays a key role in the activation of FtsWI which we designate AWI (Activation of FtsWI) and present evidence that FtsL acts through FtsI. Our results suggest that FtsN switches FtsQLB from a recruitment complex to an activator with FtsL interacting with FtsI to activate FtsW. Since FtsQLB and FtsWI are widely conserved in bacteria this mechanism is likely to be also widely conserved.SignificanceA critical step in bacterial cytokinesis is the activation of septal peptidoglycan synthesis at the Z ring. Although FtsN is the trigger and acts through FtsQLB and FtsA to activate FtsWI the mechanism is unclear. Here we find an essential role for FtsL in activating septal PG synthesis and find that it acts on FtsI. Our results suggest a model where FtsWI is recruited in an inactive form by FtsQLB and upon FtsN arrival, FtsQLB undergoes a conformational change so that a region of FtsL, that we designate the AWI domain, becomes available to interact with FtsI and activate the FtsWI complex. This mechanism for activation of the divisome has similarities to activation of the elongasome and is likely to be widely conserved in bacteria.

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Structural Analysis of the Interaction between the Bacterial Cell Division Proteins FtsQ and FtsB

Cited by 42 publications

References 43 publications

Structural Insights into the FtsQ/FtsB/FtsL Complex, a Key Component of the Divisome

Structural Insights into the FtsQ/FtsB/FtsL Complex, a Key Component of the Divisome

Cyclic AMP-CRP Modulates the Cell Morphology of Klebsiella pneumoniae in High-Glucose Environment

Essential role for FtsL in activation of septal PG synthesis

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