ArticleJournal of bacteriology1997
Domain-swapping analysis of FtsI, FtsL, and FtsQ, bitopic membrane proteins essential for cell division in Escherichia coli.
Article in Journal of bacteriology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
53 citing papers in PubMed, 103 citations in OpenAlex.
- Control of morphogenesis during theScience advances · 2025Article
- Article
- Article
- Role of the antiparallel double-stranded filament form of FtsA in activating thebioRxiv : the preprint server for biology · 2024Article
- Relationship between the Rod complex and peptidoglycan structure in Escherichia coli.MicrobiologyOpen · 2023Article
- Molecular basis for the reversible ADP-ribosylation of guanosine bases.Molecular cell · 2023Article
- New biochemistry in the Rhodanese-phosphatase superfamily: emerging roles in diverse metabolic processes, nucleic acid modifications, and biological conflicts.NAR genomics and bioinformatics · 2023Article
- Localization, Assembly, and Activation of the Escherichia coli Cell Division Machinery.EcoSal Plus · 2021Review
- Article
- pH-dependent activation of cytokinesis modulates Escherichia coli cell size.PLoS genetics · 2020Article
- The FtsLB subcomplex of the bacterial divisome is a tetramer with an uninterrupted FtsL helix linking the transmembrane and periplasmic regions.The Journal of biological chemistry · 2018Article
- Assembly and activation of the Escherichia coli divisome.Molecular microbiology · 2017Review
- Screening for transmembrane association in divisome proteins using TOXGREEN, a high-throughput variant of the TOXCAT assay.Biochimica et biophysica acta · 2016Article
- Targeting the Bacterial Division Protein FtsZ.Journal of medicinal chemistry · 2016Review
- The Soluble Periplasmic Domains of Escherichia coli Cell Division Proteins FtsQ/FtsB/FtsL Form a Trimeric Complex with Submicromolar Affinity.The Journal of biological chemistry · 2015Article
- A role for FtsA in SPOR-independent localization of the essential Escherichia coli cell division protein FtsN.Molecular microbiology · 2014Article
- Fine-mapping the contact sites of the Escherichia coli cell division proteins FtsB and FtsL on the FtsQ protein.The Journal of biological chemistry · 2013Article
- Role of leucine zipper motifs in association of the Escherichia coli cell division proteins FtsL and FtsB.Journal of bacteriology · 2011Article
- A model for the Escherichia coli FtsB/FtsL/FtsQ cell division complex.BMC structural biology · 2011Article
- Multiple interaction domains in FtsL, a protein component of the widely conserved bacterial FtsLBQ cell division complex.Journal of bacteriology · 2010Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
FtsI, FtsL, and FtsQ are three membrane proteins required for assembly of the division septum in the bacterium Escherichia coli. Cells lacking any of these three proteins form long, aseptate filaments that eventually lyse. FtsI, FtsL, and FtsQ are not homologous but have similar overall structures: a small cytoplasmic domain, a single membrane-spanning segment (MSS), and a large periplasmic domain that probably encodes the primary functional activities of these proteins. The periplasmic domain of FtsI catalyzes transpeptidation and is involved in the synthesis of septal peptidoglycan. The precise functions of FtsL and FtsQ are not known. To ask whether the cytoplasmic domain and MSS of each protein serve only as a membrane anchor or have instead a more sophisticated function, we have used molecular genetic techniques to swap these domains among the three Fts proteins and one membrane protein not involved in cell division, MalF. In the cases of FtsI and FtsL, replacement of the cytoplasmic domain and/or MSS resulted in the loss of the ability to support cell division. For FtsQ, MSS swaps supported cell division but cytoplasmic domain swaps did not. We discuss several potential interpretations of these results, including that the essential domains of FtsI, FtsL, and FtsQ have a role in regulating the localization and/or activity of these proteins to ensure that septum formation occurs at the right place in the cell and at the right time during the division cycle.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.