Evidence map›Paper›PMID 36151380›Full record

ArticleSub-cellular biochemistry2022

Regulation of Lytic Machineries by the FtsEX Complex in the Bacterial Divisome.

Martín Alcorlo, Siseth Martínez-Caballero, Rafael Molina, Juan A Hermoso

Abstract read
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In one paragraph

Article in Sub-cellular biochemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
10.9field-weighted citation impact, top 1% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

3 citing papers in PubMed, 10 citations in OpenAlex.

  1. Review
  2. Article
  3. Mechanistic insights into the regulation of cell wall hydrolysis by FtsEX and EnvC at the bacterial division site.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 1 institution in 2 countries.

Martín AlcorloDepartment of Crystallography and Structural Biology, Institute of Physical Chemistry "Rocasolano", CSIC, Madrid, Spain.
Siseth Martínez-CaballeroDepartment of Crystallography and Structural Biology, Institute of Physical Chemistry "Rocasolano", CSIC, Madrid, Spain.
Rafael MolinaDepartment of Crystallography and Structural Biology, Institute of Physical Chemistry "Rocasolano", CSIC, Madrid, Spain.
Juan A HermosoDepartment of Crystallography and Structural Biology, Institute of Physical Chemistry "Rocasolano", CSIC, Madrid, Spain. xjuan@iqfr.csic.es.
Instituto de Química Física Blas Cabrera · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The essential membrane complex FtsE/FtsX (FtsEX), belonging to the ABC transporter superfamily and widespread among bacteria, plays a relevant function in some crucial cell wall remodeling processes such as cell division, elongation, or sporulation. FtsEX plays a double role by recruiting proteins to the divisome apparatus and by regulating lytic activity of the cell wall hydrolases required for daughter cell separation. Interestingly, FtsEX does not act as a transporter but uses the ATPase activity of FtsE to mechanically transmit a signal from the cytosol, through the membrane, to the periplasm that activates the attached hydrolases. While the complete molecular details of such mechanism are not yet known, evidence has been recently reported that clarify essential aspects of this complex system. In this chapter we will present recent structural advances on this topic. The three-dimensional structure of FtsE, FtsX, and some of the lytic enzymes or their cognate regulators revealed an unexpected scenario in which a delicate set of intermolecular interactions, conserved among different bacterial genera, could be at the core of this regulatory mechanism providing exquisite control in both space and time of this central process to assist bacterial survival.

Indexed as

Bacterial ProteinsEscherichia coli ProteinsAdenosine TriphosphatasesATP-Binding Cassette TransportersBacteriaCell Cycle ProteinsProtein BindingAdenosine TriphosphatasesATP-Binding Cassette TransportersBacterial ProteinsCell Cycle ProteinsEscherichia coli Proteins3D structureABC transportersBacterial divisionDivisomeFtsEFtsXLytic regulationMechano-transmissionPcsBSPOR

Identifiers

PMID36151380
OpenAlexW4297030322

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.