Literature DB >> 20460179

FtsQ interaction mutants: a way to identify new antibacterial targets.

L Grenga1, G Guglielmi, S Melino, P Ghelardini, L Paolozzi.   

Abstract

FtsQ is a highly conserved component of the divisome that plays a central role in the assembly of early and late cell division proteins. The biological activity of this protein is still largely unknown, but its ability to interact with many components of the divisome was described by both two-hybrid assays and co-immunoprecipitation experiments. This paper describes the behaviour of ftsQ point mutants, created by random mutagenesis without regard to their phenotype, in which FtsQ is impaired in its ability to interact with its Escherichia coli division partners. Our results allow the identification of FtsQ residues involved in the interaction with other partner proteins and the determination of the biological significance of these interactions. The knowledge derived by this study could constitute not only the basis for understanding how these proteins assemble in the divisome, but also a starting point for the design of new antibacterial drugs that disrupt the bacterial division machinery.
Copyright © 2010 Elsevier B.V. All rights reserved.

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Year:  2010        PMID: 20460179     DOI: 10.1016/j.nbt.2010.05.002

Source DB:  PubMed          Journal:  N Biotechnol        ISSN: 1871-6784            Impact factor:   5.079


  7 in total

1.  Evidence from artificial septal targeting and site-directed mutagenesis that residues in the extracytoplasmic β domain of DivIB mediate its interaction with the divisomal transpeptidase PBP 2B.

Authors:  Susan L Rowland; Kimberly D Wadsworth; Scott A Robson; Carine Robichon; Jon Beckwith; Glenn F King
Journal:  J Bacteriol       Date:  2010-09-24       Impact factor: 3.490

2.  Fine-mapping the contact sites of the Escherichia coli cell division proteins FtsB and FtsL on the FtsQ protein.

Authors:  H Bart van den Berg van Saparoea; Marjolein Glas; Ingrid G W H Vernooij; Wilbert Bitter; Tanneke den Blaauwen; Joen Luirink
Journal:  J Biol Chem       Date:  2013-07-11       Impact factor: 5.157

3.  The Soluble Periplasmic Domains of Escherichia coli Cell Division Proteins FtsQ/FtsB/FtsL Form a Trimeric Complex with Submicromolar Affinity.

Authors:  Marjolein Glas; H Bart van den Berg van Saparoea; Stephen H McLaughlin; Winfried Roseboom; Fan Liu; Gregory M Koningstein; Alexander Fish; Tanneke den Blaauwen; Albert J R Heck; Luitzen de Jong; Wilbert Bitter; Iwan J P de Esch; Joen Luirink
Journal:  J Biol Chem       Date:  2015-07-09       Impact factor: 5.157

4.  A model for the Escherichia coli FtsB/FtsL/FtsQ cell division complex.

Authors:  Felipe Villanelo; Alexis Ordenes; Juan Brunet; Rosalba Lagos; Octavio Monasterio
Journal:  BMC Struct Biol       Date:  2011-06-14

5.  Molecular Characterization of the Burkholderia cenocepacia dcw Operon and FtsZ Interactors as New Targets for Novel Antimicrobial Design.

Authors:  Gabriele Trespidi; Viola Camilla Scoffone; Giulia Barbieri; Giovanna Riccardi; Edda De Rossi; Silvia Buroni
Journal:  Antibiotics (Basel)       Date:  2020-11-24

6.  Covalent Proteomimetic Inhibitor of the Bacterial FtsQB Divisome Complex.

Authors:  Felix M Paulussen; Gina K Schouten; Carolin Moertl; Jolanda Verheul; Irma Hoekstra; Gregory M Koningstein; George H Hutchins; Aslihan Alkir; Rosa A Luirink; Daan P Geerke; Peter van Ulsen; Tanneke den Blaauwen; Joen Luirink; Tom N Grossmann
Journal:  J Am Chem Soc       Date:  2022-08-09       Impact factor: 16.383

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

Authors:  Danguole Kureisaite-Ciziene; Aravindan Varadajan; Stephen H McLaughlin; Marjolein Glas; Alejandro Montón Silva; Rosa Luirink; Carolin Mueller; Tanneke den Blaauwen; Tom N Grossmann; Joen Luirink; Jan Löwe
Journal:  MBio       Date:  2018-09-11       Impact factor: 7.867

  7 in total

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