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Article ; Online: Cell Fractionation.

Petiti, Melissa / Houot, Laetitia / Duché, Denis

Methods in molecular biology (Clifton, N.J.)

2023 Volume 2715, Page(s) 65–71

Abstract: Protein function is generally dependent on its subcellular localization. In gram-negative bacteria such as Escherichia coli, a protein can be targeted to five different compartments: the cytoplasm, the inner membrane, the periplasm, the outer membrane, ... ...

Abstract	Protein function is generally dependent on its subcellular localization. In gram-negative bacteria such as Escherichia coli, a protein can be targeted to five different compartments: the cytoplasm, the inner membrane, the periplasm, the outer membrane, and the extracellular medium. Different approaches can be used to determine the protein localization within cell such as in silico identification of protein signal sequences and motifs, electron microscopy and immunogold labeling, optical fluorescence microscopy, and biochemical technics. In this chapter, we describe a simple and efficient method to isolate the different compartments of Escherichia coli by a fractionation method and to determine the presence of the protein of interest. For inner membrane proteins, we propose a method to discriminate between integral and peripheral membrane proteins.
MeSH term(s)	Cell Fractionation ; Chemical Fractionation ; Cytoplasm ; Escherichia coli ; Membrane Proteins
Chemical Substances	Membrane Proteins
Language	English
Publishing date	2023-11-06
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1940-6029
ISSN (online)	1940-6029
DOI	10.1007/978-1-0716-3445-5_3
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Article ; Online: Protein-Protein Interactions: Oxidative Bacterial Two Hybrid.

Pellegri, Callypso / Bouveret, Emmanuelle / Houot, Laetitia

Methods in molecular biology (Clifton, N.J.)

2023 Volume 2715, Page(s) 225–233

Abstract: Protein-protein interaction studies are essential to understand how proteins organize themselves into interaction networks and thus influence cellular processes. Protein binding specificity depends on the correct three-dimensional folding of the ... ...

Abstract	Protein-protein interaction studies are essential to understand how proteins organize themselves into interaction networks and thus influence cellular processes. Protein binding specificity depends on the correct three-dimensional folding of the polypeptide sequences. One of the forces involved in the structuring and stability of proteins is the formation of disulfide bonds. These covalent bonds are formed posttranscriptionally by the oxidation of a pair of cysteine residues and can serve structural, catalytic, or signaling roles. Here, we describe an engineered E. coli adenylate cyclase mutant strain with an oxidative cytoplasm that promotes correct folding of proteins with disulfide bonds. This genetic background expands the set of host strains suitable for studying protein-protein interactions in vivo by the adenylate cyclase two-hybrid approach.
MeSH term(s)	Adenylyl Cyclases ; Escherichia coli/genetics ; Oxidation-Reduction ; Disulfides ; Oxidative Stress
Chemical Substances	Adenylyl Cyclases (EC 4.6.1.1) ; Disulfides
Language	English
Publishing date	2023-11-06
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1940-6029
ISSN (online)	1940-6029
DOI	10.1007/978-1-0716-3445-5_14
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Article ; Online: Direct interaction between fd phage pilot protein pIII and the TolQ-TolR proton-dependent motor provides new insights into the import of filamentous phages.

Pellegri, Callypso / Moreau, Ambre / Duché, Denis / Houot, Laetitia

The Journal of biological chemistry

2023 Volume 299, Issue 8, Page(s) 105048

Abstract: Filamentous phages are one of the simplest examples of viruses with a protein capsid that protects a circular single-stranded DNA genome. The infection is very specific, nonlytic, and can strongly affect the physiology or provide new pathogenic factors ... ...

Abstract	Filamentous phages are one of the simplest examples of viruses with a protein capsid that protects a circular single-stranded DNA genome. The infection is very specific, nonlytic, and can strongly affect the physiology or provide new pathogenic factors to its bacterial host. The infection process is proposed to rely on a pore-forming mechanism similar to that of certain nonenveloped eukaryotic viruses. The Ff coliphages (including M13, fd, and f1) have been intensively studied and were used to establish the sequence of events taking place for efficient crossing of the host envelope structure. However, the mechanism involved in the penetration of the cell inner membrane is not well understood. Here, we identify new host players involved in the phage translocation mechanism. Interaction studies by a combination of in vivo biochemical methods demonstrate that the adhesion protein pIII located at the tip of the phage binds to TolQ and TolR, two proteins that form a conserved proton-dependent molecular motor in the inner membrane of the host cell. Moreover, in vivo cysteine cross-linking studies reveal that the interactions between the pIII and TolQ or TolR occur between their transmembrane helix domains and may be responding to the proton motive force status of the cell. These results allow us to propose a model for the late stage of filamentous phage translocation mediated by multiple interactions with each individual component of the host TolQRA complex.
MeSH term(s)	Bacteriophage M13 ; Escherichia coli/genetics ; Escherichia coli/metabolism ; Escherichia coli Proteins/metabolism ; Membrane Proteins/metabolism ; Protons ; Viral Proteins/metabolism
Chemical Substances	Escherichia coli Proteins ; Membrane Proteins ; Protons ; tolQ protein, E coli (110736-92-0) ; tolR protein, E coli (110736-93-1) ; Viral Proteins
Language	English
Publishing date	2023-07-13
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1016/j.jbc.2023.105048
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Article ; Online: Similarities and Differences between Colicin and Filamentous Phage Uptake by Bacterial Cells.

Duché, Denis / Houot, Laetitia

EcoSal Plus

2019 Volume 8, Issue 2

Abstract: Gram-negative bacteria have evolved a complex envelope to adapt and survive in a broad range of ecological niches. This physical barrier is the first line of defense against noxious compounds and viral particles called bacteriophages. Colicins are a ... ...

Abstract	Gram-negative bacteria have evolved a complex envelope to adapt and survive in a broad range of ecological niches. This physical barrier is the first line of defense against noxious compounds and viral particles called bacteriophages. Colicins are a family of bactericidal proteins produced by and toxic to
MeSH term(s)	Bacteria/metabolism ; Bacteria/virology ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Biological Transport ; Colicins/metabolism ; Coliphages/metabolism ; Escherichia coli/metabolism ; Escherichia coli Proteins/metabolism ; Host Microbial Interactions ; Multiprotein Complexes ; Periplasmic Proteins ; Protein Binding ; Protein Transport
Chemical Substances	Bacterial Proteins ; Colicins ; Escherichia coli Proteins ; Multiprotein Complexes ; Periplasmic Proteins
Language	English
Publishing date	2019-03-26
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ISSN	2324-6200
ISSN (online)	2324-6200
DOI	10.1128/ecosalplus.ESP-0030-2018
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Article ; Online: Interpretation of 2-[

Manson, Guillaume / Lemchukwu, Amaeshi Chukwunonye / Mokrane, Fatima-Zohra / Lopci, Egesta / Aide, Nicolas / Vercellino, Laetitia / Houot, Roch / Dercle, Laurent

European radiology

2022 Volume 32, Issue 9, Page(s) 6536–6544

Abstract: The development of immunotherapy has revolutionized cancer treatment, improving the outcome and survival of many patients. Immune checkpoint inhibitors (ICIs), the most common form of immunotherapy, use antibodies to restore T-cells' anti-tumor activity. ...

Abstract	The development of immunotherapy has revolutionized cancer treatment, improving the outcome and survival of many patients. Immune checkpoint inhibitors (ICIs), the most common form of immunotherapy, use antibodies to restore T-cells' anti-tumor activity. Immune checkpoint inhibitors are gaining ground in the therapeutic strategy across various cancers. Although widely used in solid tumors, ICIs have shown remarkable efficacy in patients with Hodgkin lymphoma. 2-[
MeSH term(s)	Fluorodeoxyglucose F18 ; Hodgkin Disease/diagnostic imaging ; Hodgkin Disease/drug therapy ; Humans ; Immune Checkpoint Inhibitors ; Positron Emission Tomography Computed Tomography/methods ; Positron-Emission Tomography ; Tomography, X-Ray Computed
Chemical Substances	Immune Checkpoint Inhibitors ; Fluorodeoxyglucose F18 (0Z5B2CJX4D)
Language	English
Publishing date	2022-03-28
Publishing country	Germany
Document type	Journal Article ; Review
ZDB-ID	1085366-2
ISSN	1432-1084 ; 0938-7994 ; 1613-3749
ISSN (online)	1432-1084
ISSN	0938-7994 ; 1613-3749
DOI	10.1007/s00330-022-08669-8
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Article ; Online: Timing of TolA and TolQ Recruitment at the Septum Depends on the Functionality of the Tol-Pal System.

Baccelli, Pauline / Rachedi, Raphaël / Serrano, Bastien / Petiti, Mélissa / Bernard, Christophe S / Houot, Laetitia / Duche, Denis

Journal of molecular biology

2022 Volume 434, Issue 7, Page(s) 167519

Abstract: Efficient cell division of Gram-negative bacteria requires the presence of the Tol-Pal system to coordinate outer membrane (OM) invagination with inner membrane invagination (IM) and peptidoglycan (PG) remodeling. The Tol-Pal system is a trans-envelope ... ...

Abstract	Efficient cell division of Gram-negative bacteria requires the presence of the Tol-Pal system to coordinate outer membrane (OM) invagination with inner membrane invagination (IM) and peptidoglycan (PG) remodeling. The Tol-Pal system is a trans-envelope complex that connects the three layers of the cell envelope through an energy-dependent process. It is composed of the three IM proteins, TolA, TolQ and TolR, the periplasmic protein TolB and the OM lipoprotein Pal. The proteins of the Tol-Pal system are dynamically recruited to the cell septum during cell division. TolA, the central hub of the Tol-Pal system, has three domains: a transmembrane helix (TolA
MeSH term(s)	Bacterial Outer Membrane Proteins/metabolism ; Cell Division ; Escherichia coli/cytology ; Escherichia coli/metabolism ; Escherichia coli Proteins/metabolism ; Lipoproteins/metabolism ; Peptidoglycan/metabolism
Chemical Substances	Bacterial Outer Membrane Proteins ; Escherichia coli Proteins ; ExcC protein, E coli ; Lipoproteins ; Peptidoglycan ; tolA protein, E coli ; tolQ protein, E coli (110736-92-0)
Language	English
Publishing date	2022-02-28
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	80229-3
ISSN	1089-8638 ; 0022-2836
ISSN (online)	1089-8638
ISSN	0022-2836
DOI	10.1016/j.jmb.2022.167519
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Article ; Online: The Tol-Pal system of Escherichia coli plays an unexpected role in the import of the oxyanions chromate and phosphate.

Ali Chaouche, Amine / Houot, Laetitia / Duché, Denis / Iobbi-Nivol, Chantal / Giudici-Orticoni, Marie-Thérèse / Fons, Michel / Méjean, Vincent

Research in microbiology

2022 Volume 173, Issue 8, Page(s) 103967

Abstract: Chromate is a toxic metal that enters bacteria by using oxyanion importers. Here, we show that each mutant of the Tol-Pal system of Escherichia coli exhibited increased chromate resistance. This system, which spans the cell envelope, plays a major role ... ...

Abstract	Chromate is a toxic metal that enters bacteria by using oxyanion importers. Here, we show that each mutant of the Tol-Pal system of Escherichia coli exhibited increased chromate resistance. This system, which spans the cell envelope, plays a major role in envelope integrity and septation. The ΔtolQR mutant accumulated three-fold less chromate than the wild-type. Addition of phosphate but not sulfate to rich medium drastically reduced chromate toxicity and import in the wild-type strain. Furthermore, the intracellular concentration of free inorganic phosphate was significantly reduced for the ΔtolR mutant in comparison to the wild-type strain. Moreover, extracellular labeled phosphate was significantly less incorporated into the ΔtolR mutant. Finally, two distinct TolQR mutant complexes, specifically affected in Tol-Pal energization without affecting the TolQRA complex structure, did not complement the ΔtolQR mutant for inorganic phosphate accumulation. We thus propose that, while the Pst system is well known to import inorganic phosphate, the Tol-Pal system participates to phosphate uptake in particular at medium to high extracellular phosphate concentrations. Since mutations disabling the Tol-Pal system lead to pleiotropic effects, chromate resistance and reduced inorganic phosphate import could occur from an indirect effect of mutations in components of the Tol-Pal system.
MeSH term(s)	Escherichia coli/genetics ; Escherichia coli Proteins/genetics ; Chromates ; Phosphates
Chemical Substances	Escherichia coli Proteins ; Chromates ; Phosphates
Language	English
Publishing date	2022-06-01
Publishing country	France
Document type	Journal Article
ZDB-ID	1004220-9
ISSN	1769-7123 ; 0923-2508
ISSN (online)	1769-7123
ISSN	0923-2508
DOI	10.1016/j.resmic.2022.103967
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Article ; Online: Decoupling Filamentous Phage Uptake and Energy of the TolQRA Motor in Escherichia coli.

Samire, Poutoum / Serrano, Bastien / Duché, Denis / Lemarié, Emeline / Lloubès, Roland / Houot, Laetitia

Journal of bacteriology

2020 Volume 202, Issue 2

Abstract: Filamentous phages are nonlytic viruses that specifically infect bacteria, establishing a persistent association with their host. The phage particle has no machinery for generating energy and parasitizes its host's existing structures in order to cross ... ...

Abstract	Filamentous phages are nonlytic viruses that specifically infect bacteria, establishing a persistent association with their host. The phage particle has no machinery for generating energy and parasitizes its host's existing structures in order to cross the bacterial envelope and deliver its genetic material. The import of filamentous phages across the bacterial periplasmic space requires some of the components of a macrocomplex of the envelope known as the Tol system. This complex uses the energy provided by the proton motive force (pmf) of the inner membrane to perform essential and highly energy-consuming functions of the cell, such as envelope integrity maintenance and cell division. It has been suggested that phages take advantage of pmf-driven conformational changes in the Tol system to transit across the periplasm. However, this hypothesis has not been formally tested. In order to decouple the role of the Tol system in cell physiology and during phage parasitism, we used mutations on conserved essential residues known for inactivating pmf-dependent functions of the Tol system. We identified impaired Tol complexes that remain fully efficient for filamentous phage uptake. We further demonstrate that the TolQ-TolR homologous motor ExbB-ExbD, normally operating with the TonB protein, is able to promote phage infection along with full-length TolA.
MeSH term(s)	Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Bacteriophages/metabolism ; Escherichia coli/genetics ; Escherichia coli/metabolism ; Escherichia coli Proteins/genetics ; Escherichia coli Proteins/metabolism ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Proton-Motive Force/genetics ; Proton-Motive Force/physiology
Chemical Substances	Bacterial Proteins ; Escherichia coli Proteins ; ExbB protein, E coli ; Membrane Proteins ; tolQ protein, E coli (110736-92-0) ; tolR protein, E coli (110736-93-1) ; exbD protein, E coli (123424-75-9)
Language	English
Publishing date	2020-01-02
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2968-3
ISSN	1098-5530 ; 0021-9193
ISSN (online)	1098-5530
ISSN	0021-9193
DOI	10.1128/JB.00428-19
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Article: The Tol-Pal system of Escherichia coli plays an unexpected role in the import of the oxyanions chromate and phosphate

Chaouche, Amine Ali / Houot, Laetitia / Duché, Denis / Iobbi-Nivol, Chantal / Giudici-Orticoni, Marie-Thérèse / Fons, Michel / Méjean, Vincent

Research in microbiology. 2022 May 24,

2022

Abstract	Chromate is a toxic metal that enters bacteria by using oxyanion importers. Here, we show that each mutant of the Tol-Pal system of Escherichia coli exhibited increased chromate resistance. This system, which spans the cell envelope, plays a major role in envelope integrity and septation. The ΔtolQR mutant accumulated three-fold less chromate than the wild-type. Addition of phosphate but not sulfate to rich medium drastically reduced chromate toxicity and import in the wild-type strain. Furthermore, the intracellular concentration of free inorganic phosphate was significantly reduced for the ΔtolR mutant in comparison to the wild-type strain. Moreover, extracellular labelled phosphate was significantly less incorporated into the ΔtolR mutant. Finally, two distinct TolQR mutant complexes, specifically affected in Tol-Pal energization without affecting the TolQRA complex structure, did not complement the ΔtolQR mutant for inorganic phosphate accumulation. We thus propose that, while the Pst system is well known to import inorganic phosphate, the Tol-Pal system participates to phosphate uptake in particular at medium to high extracellular phosphate concentrations. Since mutations disabling the Tol-Pal system lead to pleiotropic effects, chromate resistance and reduced inorganic phosphate import could occur from an indirect effect of mutations in components of the Tol-Pal system.
Keywords	Escherichia coli ; chromates ; imports ; mutants ; oxyanions ; phosphates ; research ; sulfates ; toxicity
Language	English
Dates of publication	2022-0524
Publishing place	Elsevier Masson SAS
Document type	Article
Note	Pre-press version
ZDB-ID	1004220-9
ISSN	1769-7123 ; 0923-2508
ISSN (online)	1769-7123
ISSN	0923-2508
DOI	10.1016/j.resmic.2022.103967
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Article: Timing of TolA and TolQ Recruitment at the Septum Depends on the Functionality of the Tol-Pal System

Baccelli, Pauline / Rachedi, Raphaël / Serrano, Bastien / Petiti, Mélissa / Bernard, Christophe S / Houot, Laetitia / Duche, Denis

Journal of molecular biology. 2022 Apr. 15, v. 434, no. 7

2022

Abstract	Efficient cell division of Gram-negative bacteria requires the presence of the Tol-Pal system to coordinate outer membrane (OM) invagination with inner membrane invagination (IM) and peptidoglycan (PG) remodeling. The Tol-Pal system is a trans-envelope complex that connects the three layers of the cell envelope through an energy-dependent process. It is composed of the three IM proteins, TolA, TolQ and TolR, the periplasmic protein TolB and the OM lipoprotein Pal. The proteins of the Tol-Pal system are dynamically recruited to the cell septum during cell division. TolA, the central hub of the Tol-Pal system, has three domains: a transmembrane helix (TolA₁), a long second helical periplasmic domain (TolA₂) and a C-terminal globular domain (TolA₃). The TolQR complex uses the PMF to energize TolA, allowing its cyclic interaction via TolA₃ with the OM TolB-Pal complex. Here, we confirm that TolA₂ is sufficient to address TolA to the site of constriction, whereas TolA₁ is recruited by TolQ. Analysis of the protein localization as function of the bacterial cell age revealed that TolA and TolQ localize earlier at midcell in the absence of the other Tol-Pal proteins. These data suggest that TolA and TolQ are delayed from their septal recruitment by the multiple interactions of TolA with TolB-Pal in the cell envelope providing a new example of temporal regulation of proteins recruitment at the septum.
Keywords	cell division ; lipoproteins ; molecular biology ; peptidoglycans
Language	English
Dates of publication	2022-0415
Publishing place	Elsevier Ltd
Document type	Article
ZDB-ID	80229-3
ISSN	1089-8638 ; 0022-2836
ISSN (online)	1089-8638
ISSN	0022-2836
DOI	10.1016/j.jmb.2022.167519
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