Essential Role for FtsL in Activation of Septal Peptidoglycan Synthesis

ABSTRACT Spatiotemporal regulation of septal peptidoglycan (PG) synthesis is achieved by coupling assembly and activation of the synthetic enzymes (FtsWI) to the Z ring, a cytoskeletal element that is required for division in most bacteria. In Escherichia coli, the recruitment of the FtsWI complex i...

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Autores principales: Kyung-Tae Park, Shishen Du, Joe Lutkenhaus
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Publicado: American Society for Microbiology 2020
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spelling oai:doaj.org-article:e9921a38a5904d918b2c72dcc68f69c52021-11-15T15:55:44ZEssential Role for FtsL in Activation of Septal Peptidoglycan Synthesis10.1128/mBio.03012-202150-7511https://doaj.org/article/e9921a38a5904d918b2c72dcc68f69c52020-12-01T00:00:00Zhttps://journals.asm.org/doi/10.1128/mBio.03012-20https://doaj.org/toc/2150-7511ABSTRACT Spatiotemporal regulation of septal peptidoglycan (PG) synthesis is achieved by coupling assembly and activation of the synthetic enzymes (FtsWI) to the Z ring, a cytoskeletal element that is required for division in most bacteria. In Escherichia 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, which 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. IMPORTANCE A 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 peptidoglycan (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 the arrival of FtsN, FtsQLB undergoes a conformational change so that a region of FtsL, which 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 the activation of the elongasome and is likely to be widely conserved in bacteria.Kyung-Tae ParkShishen DuJoe LutkenhausAmerican Society for Microbiologyarticlecell divisiondivisomeseptal ringseptationMicrobiologyQR1-502ENmBio, Vol 11, Iss 6 (2020)
institution DOAJ
collection DOAJ
language EN
topic cell division
divisome
septal ring
septation
Microbiology
QR1-502
spellingShingle cell division
divisome
septal ring
septation
Microbiology
QR1-502
Kyung-Tae Park
Shishen Du
Joe Lutkenhaus
Essential Role for FtsL in Activation of Septal Peptidoglycan Synthesis
description ABSTRACT Spatiotemporal regulation of septal peptidoglycan (PG) synthesis is achieved by coupling assembly and activation of the synthetic enzymes (FtsWI) to the Z ring, a cytoskeletal element that is required for division in most bacteria. In Escherichia 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, which 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. IMPORTANCE A 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 peptidoglycan (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 the arrival of FtsN, FtsQLB undergoes a conformational change so that a region of FtsL, which 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 the activation of the elongasome and is likely to be widely conserved in bacteria.
format article
author Kyung-Tae Park
Shishen Du
Joe Lutkenhaus
author_facet Kyung-Tae Park
Shishen Du
Joe Lutkenhaus
author_sort Kyung-Tae Park
title Essential Role for FtsL in Activation of Septal Peptidoglycan Synthesis
title_short Essential Role for FtsL in Activation of Septal Peptidoglycan Synthesis
title_full Essential Role for FtsL in Activation of Septal Peptidoglycan Synthesis
title_fullStr Essential Role for FtsL in Activation of Septal Peptidoglycan Synthesis
title_full_unstemmed Essential Role for FtsL in Activation of Septal Peptidoglycan Synthesis
title_sort essential role for ftsl in activation of septal peptidoglycan synthesis
publisher American Society for Microbiology
publishDate 2020
url https://doaj.org/article/e9921a38a5904d918b2c72dcc68f69c5
work_keys_str_mv AT kyungtaepark essentialroleforftslinactivationofseptalpeptidoglycansynthesis
AT shishendu essentialroleforftslinactivationofseptalpeptidoglycansynthesis
AT joelutkenhaus essentialroleforftslinactivationofseptalpeptidoglycansynthesis
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