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  1. Artikel ; Online: Cell Fractionation.

    Petiti, Melissa / Houot, Laetitia / Duché, Denis

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

    2023  Band 2715, Seite(n) 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-Begriff(e) Cell Fractionation ; Chemical Fractionation ; Cytoplasm ; Escherichia coli ; Membrane Proteins
    Chemische Substanzen Membrane Proteins
    Sprache Englisch
    Erscheinungsdatum 2023-11-06
    Erscheinungsland United States
    Dokumenttyp 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
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  2. Artikel: 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 ... ...

    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.
    Schlagwörter cell division ; lipoproteins ; molecular biology ; peptidoglycans
    Sprache Englisch
    Erscheinungsverlauf 2022-0415
    Erscheinungsort Elsevier Ltd
    Dokumenttyp Artikel
    ZDB-ID 80229-3
    ISSN 1089-8638 ; 0022-2836
    ISSN (online) 1089-8638
    ISSN 0022-2836
    DOI 10.1016/j.jmb.2022.167519
    Datenquelle NAL Katalog (AGRICOLA)

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  3. Artikel ; 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  Band 434, Heft 7, Seite(n) 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-Begriff(e) Bacterial Outer Membrane Proteins/metabolism ; Cell Division ; Escherichia coli/cytology ; Escherichia coli/metabolism ; Escherichia coli Proteins/metabolism ; Lipoproteins/metabolism ; Peptidoglycan/metabolism
    Chemische Substanzen Bacterial Outer Membrane Proteins ; Escherichia coli Proteins ; ExcC protein, E coli ; Lipoproteins ; Peptidoglycan ; tolA protein, E coli ; tolQ protein, E coli (110736-92-0)
    Sprache Englisch
    Erscheinungsdatum 2022-02-28
    Erscheinungsland Netherlands
    Dokumenttyp 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
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

    Volltext online

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    Verfügbar in ZB MED Köln/Königswinter

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  4. Artikel ; Online: Cell Fractionation.

    Petiti, Melissa / Houot, Laetitia / Duché, Denis

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

    2017  Band 1615, Seite(n) 59–64

    Abstract: Protein function is generally dependent on its subcellular localisation. 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 localisation. 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 localisation within a cell such as in silico identification of protein signal sequences and motifs, electron microscopy and immunogold labelling, 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-Begriff(e) Bacterial Proteins/chemistry ; Bacterial Proteins/metabolism ; Cell Fractionation/methods ; Escherichia coli/chemistry ; Gram-Negative Bacteria/chemistry ; Solubility
    Chemische Substanzen Bacterial Proteins
    Sprache Englisch
    Erscheinungsdatum 2017
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 1940-6029
    ISSN (online) 1940-6029
    DOI 10.1007/978-1-4939-7033-9_3
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  5. Artikel: Tol Energy-Driven Localization of Pal and Anchoring to the Peptidoglycan Promote Outer-Membrane Constriction

    Petiti, Mélissa / Serrano, Bastien / Faure, Laura / Lloubes, Roland / Mignot, Tâm / Duché, Denis

    Journal of molecular biology. 2019 Aug. 09, v. 431, no. 17

    2019  

    Abstract: During cell division, gram-negative bacteria must coordinate inner-membrane invagination, peptidoglycan synthesis and cleavage and outer-membrane (OM) constriction. The OM constriction remains largely enigmatic, and the nature of this process, passive or ...

    Abstract During cell division, gram-negative bacteria must coordinate inner-membrane invagination, peptidoglycan synthesis and cleavage and outer-membrane (OM) constriction. The OM constriction remains largely enigmatic, and the nature of this process, passive or active, is under debate. The proton-motive force-dependent Tol–Pal system performs a network of interactions within these three compartments. Here we confirm that the trans-envelope Tol–Pal complex accumulates at constriction site in Escherichia coli. We show that the inner-membrane complex composed of TolA, TolQ and TolR recruits the OM complex TolB–Pal to the septum, in an energy-dependent process. Pal recruitment then allows its binding to peptidoglycan and subsequently OM constriction. Our results provide evidence that the constriction of the OM is an energized process.
    Schlagwörter Escherichia coli ; Gram-negative bacteria ; cell division ; peptidoglycans
    Sprache Englisch
    Erscheinungsverlauf 2019-0809
    Umfang p. 3275-3288.
    Erscheinungsort Elsevier Ltd
    Dokumenttyp Artikel
    ZDB-ID 80229-3
    ISSN 1089-8638 ; 0022-2836
    ISSN (online) 1089-8638
    ISSN 0022-2836
    DOI 10.1016/j.jmb.2019.05.039
    Datenquelle NAL Katalog (AGRICOLA)

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    Verfügbar in ZB MED Bonn

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  6. Artikel ; Online: Tol Energy-Driven Localization of Pal and Anchoring to the Peptidoglycan Promote Outer-Membrane Constriction.

    Petiti, Mélissa / Serrano, Bastien / Faure, Laura / Lloubes, Roland / Mignot, Tâm / Duché, Denis

    Journal of molecular biology

    2019  Band 431, Heft 17, Seite(n) 3275–3288

    Abstract: During cell division, gram-negative bacteria must coordinate inner-membrane invagination, peptidoglycan synthesis and cleavage and outer-membrane (OM) constriction. The OM constriction remains largely enigmatic, and the nature of this process, passive or ...

    Abstract During cell division, gram-negative bacteria must coordinate inner-membrane invagination, peptidoglycan synthesis and cleavage and outer-membrane (OM) constriction. The OM constriction remains largely enigmatic, and the nature of this process, passive or active, is under debate. The proton-motive force-dependent Tol-Pal system performs a network of interactions within these three compartments. Here we confirm that the trans-envelope Tol-Pal complex accumulates at constriction site in Escherichia coli. We show that the inner-membrane complex composed of TolA, TolQ and TolR recruits the OM complex TolB-Pal to the septum, in an energy-dependent process. Pal recruitment then allows its binding to peptidoglycan and subsequently OM constriction. Our results provide evidence that the constriction of the OM is an energized process.
    Mesh-Begriff(e) Bacterial Outer Membrane Proteins/chemistry ; Bacterial Outer Membrane Proteins/metabolism ; Cell Division ; Cloning, Molecular ; Escherichia coli/genetics ; Escherichia coli/metabolism ; Escherichia coli Proteins/chemistry ; Escherichia coli Proteins/genetics ; Escherichia coli Proteins/metabolism ; Lipoproteins/chemistry ; Membrane Proteins ; Multigene Family ; Peptidoglycan/chemistry
    Chemische Substanzen Bacterial Outer Membrane Proteins ; Escherichia coli Proteins ; ExcC protein, E coli ; Lipoproteins ; Membrane Proteins ; Peptidoglycan ; tolA protein, E coli ; tolQ protein, E coli (110736-92-0) ; tolR protein, E coli (110736-93-1)
    Sprache Englisch
    Erscheinungsdatum 2019-05-31
    Erscheinungsland England
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 80229-3
    ISSN 1089-8638 ; 0022-2836
    ISSN (online) 1089-8638
    ISSN 0022-2836
    DOI 10.1016/j.jmb.2019.05.039
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

    Volltext online

    Zusatzmaterialien

    Kategorien

    Verfügbar in ZB MED Köln/Königswinter

    Zs.A 867: Hefte anzeigen Standort:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

    Über subito bestellen

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