Skip to main content
bioRxiv
  • Home
  • About
  • Submit
  • ALERTS / RSS
Advanced Search
New Results

The coiled-coil domain of E. coli FtsLB is a structurally detuned element critical for modulating its activation in bacterial cell division

View ORCID ProfileSamuel J. Craven, View ORCID ProfileSamson G.F. Condon, View ORCID ProfileGladys Diaz-Vazquez, View ORCID ProfileQiang Cui, View ORCID ProfileAlessandro Senes
doi: https://doi.org/10.1101/2021.04.21.440662
Samuel J. Craven
1Department of Biochemistry, University of Wisconsin-Madison, Madison, WI 53706
2Integrated Program in Biochemistry, University of Wisconsin-Madison, Madison, WI 53706
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
  • ORCID record for Samuel J. Craven
Samson G.F. Condon
1Department of Biochemistry, University of Wisconsin-Madison, Madison, WI 53706
2Integrated Program in Biochemistry, University of Wisconsin-Madison, Madison, WI 53706
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
  • ORCID record for Samson G.F. Condon
Gladys Diaz-Vazquez
1Department of Biochemistry, University of Wisconsin-Madison, Madison, WI 53706
3Biophysics Graduate Program, University of Wisconsin-Madison, Madison, WI 53706
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
  • ORCID record for Gladys Diaz-Vazquez
Qiang Cui
4Department of Chemistry, Boston University
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
  • ORCID record for Qiang Cui
Alessandro Senes
1Department of Biochemistry, University of Wisconsin-Madison, Madison, WI 53706
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
  • ORCID record for Alessandro Senes
  • For correspondence: senes@wisc.edu
  • Abstract
  • Full Text
  • Info/History
  • Metrics
  • Preview PDF
Loading

Abstract

The FtsLB complex is a key regulator of bacterial cell division, existing in either an off or on state which supports the activation of septal peptidoglycan synthesis. In Escherichia coli, residues known to be critical for this activation are located in a region near the C-terminal end of the periplasmic coiled-coil domain of FtsLB, raising questions about the precise role of this conserved domain in the activation mechanism. Here, we investigate an unusual cluster of polar amino acids found within the core of the FtsLB coiled coil. We hypothesized that these amino acids likely reduce the structural stability of the domain and thus may be important for governing conformational changes. We found that mutating these positions to hydrophobic residues increased the thermal stability of FtsLB but caused cell division defects, suggesting that the coiled-coil domain is a “detuned” structural element. In addition, we identified suppressor mutations within the polar cluster, indicating that the precise identity of the polar amino acids is important for fine-tuning the structural balance between the off and on states. We propose a revised structural model of the tetrameric FtsLB (named the “Y-model”) in which the periplasmic domain splits into a pair of coiled-coil branches. In this configuration, the hydrophilic terminal moieties of the polar amino acids remain more favorably exposed to water than in the original four-helix bundle model (“I-model”). We propose that a shift in this architecture, dependent on its marginal stability, is involved in activating the FtsLB complex and triggering septal cell wall reconstruction.

Competing Interest Statement

The authors have declared no competing interest.

Footnotes

  • Minor revision of title and abstract

Copyright 
The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under a CC-BY-NC 4.0 International license.
Back to top
PreviousNext
Posted November 24, 2021.
Download PDF
Email

Thank you for your interest in spreading the word about bioRxiv.

NOTE: Your email address is requested solely to identify you as the sender of this article.

Enter multiple addresses on separate lines or separate them with commas.
The coiled-coil domain of E. coli FtsLB is a structurally detuned element critical for modulating its activation in bacterial cell division
(Your Name) has forwarded a page to you from bioRxiv
(Your Name) thought you would like to see this page from the bioRxiv website.
CAPTCHA
This question is for testing whether or not you are a human visitor and to prevent automated spam submissions.
Share
The coiled-coil domain of E. coli FtsLB is a structurally detuned element critical for modulating its activation in bacterial cell division
Samuel J. Craven, Samson G.F. Condon, Gladys Diaz-Vazquez, Qiang Cui, Alessandro Senes
bioRxiv 2021.04.21.440662; doi: https://doi.org/10.1101/2021.04.21.440662
Reddit logo Twitter logo Facebook logo LinkedIn logo Mendeley logo
Citation Tools
The coiled-coil domain of E. coli FtsLB is a structurally detuned element critical for modulating its activation in bacterial cell division
Samuel J. Craven, Samson G.F. Condon, Gladys Diaz-Vazquez, Qiang Cui, Alessandro Senes
bioRxiv 2021.04.21.440662; doi: https://doi.org/10.1101/2021.04.21.440662

Citation Manager Formats

  • BibTeX
  • Bookends
  • EasyBib
  • EndNote (tagged)
  • EndNote 8 (xml)
  • Medlars
  • Mendeley
  • Papers
  • RefWorks Tagged
  • Ref Manager
  • RIS
  • Zotero
  • Tweet Widget
  • Facebook Like
  • Google Plus One

Subject Area

  • Biochemistry
Subject Areas
All Articles
  • Animal Behavior and Cognition (4861)
  • Biochemistry (10811)
  • Bioengineering (8054)
  • Bioinformatics (27346)
  • Biophysics (13999)
  • Cancer Biology (11140)
  • Cell Biology (16087)
  • Clinical Trials (138)
  • Developmental Biology (8793)
  • Ecology (13307)
  • Epidemiology (2067)
  • Evolutionary Biology (17375)
  • Genetics (11694)
  • Genomics (15939)
  • Immunology (11042)
  • Microbiology (26132)
  • Molecular Biology (10669)
  • Neuroscience (56660)
  • Paleontology (420)
  • Pathology (1737)
  • Pharmacology and Toxicology (3009)
  • Physiology (4557)
  • Plant Biology (9648)
  • Scientific Communication and Education (1617)
  • Synthetic Biology (2695)
  • Systems Biology (6985)
  • Zoology (1511)