Membrane interactions and self-association of the TatA and TatB components of the twin-arginine translocation pathway

Erik De Leeuw, Ida Porcelli, Frank Sargent, Tracy Palmer, Ben C Berks

    Research output: Contribution to journalArticle

    70 Citations (Scopus)

    Abstract

    The Escherichia coli Tat system mediates Sec-independent export of protein precursors bearing twin-arginine signal peptides. The essential Tat pathway components TatA, TatB and TatC are shown to be integral membrane proteins. Upon removal of the predicted N-terminal transmembrane helix TatA becomes a water-soluble protein. In contrast the homologous TatB protein retains weak peripheral interactions with the cytoplasmic membrane when the analogous helix is deleted. Chemical crosslinking studies indicate that TatA forms at least homotrimers, and TatB minimally homodimers, in the native membrane environment. The presence of such homo-oligomeric interactions is supported by size exclusion chromatography. (C) 2001 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.

    Original languageEnglish
    Pages (from-to)143-148
    Number of pages6
    JournalFEBS Letters
    Volume506
    Issue number2
    DOIs
    Publication statusPublished - 5 Oct 2001

    Cite this

    De Leeuw, Erik ; Porcelli, Ida ; Sargent, Frank ; Palmer, Tracy ; Berks, Ben C. / Membrane interactions and self-association of the TatA and TatB components of the twin-arginine translocation pathway. In: FEBS Letters. 2001 ; Vol. 506, No. 2. pp. 143-148.
    @article{10388f6e83894f89a37f32a5e7eccb25,
    title = "Membrane interactions and self-association of the TatA and TatB components of the twin-arginine translocation pathway",
    abstract = "The Escherichia coli Tat system mediates Sec-independent export of protein precursors bearing twin-arginine signal peptides. The essential Tat pathway components TatA, TatB and TatC are shown to be integral membrane proteins. Upon removal of the predicted N-terminal transmembrane helix TatA becomes a water-soluble protein. In contrast the homologous TatB protein retains weak peripheral interactions with the cytoplasmic membrane when the analogous helix is deleted. Chemical crosslinking studies indicate that TatA forms at least homotrimers, and TatB minimally homodimers, in the native membrane environment. The presence of such homo-oligomeric interactions is supported by size exclusion chromatography. (C) 2001 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.",
    author = "{De Leeuw}, Erik and Ida Porcelli and Frank Sargent and Tracy Palmer and Berks, {Ben C}",
    year = "2001",
    month = "10",
    day = "5",
    doi = "10.1016/S0014-5793(01)02904-0",
    language = "English",
    volume = "506",
    pages = "143--148",
    journal = "FEBS Letters",
    issn = "0014-5793",
    publisher = "Wiley",
    number = "2",

    }

    Membrane interactions and self-association of the TatA and TatB components of the twin-arginine translocation pathway. / De Leeuw, Erik; Porcelli, Ida; Sargent, Frank ; Palmer, Tracy; Berks, Ben C.

    In: FEBS Letters, Vol. 506, No. 2, 05.10.2001, p. 143-148.

    Research output: Contribution to journalArticle

    TY - JOUR

    T1 - Membrane interactions and self-association of the TatA and TatB components of the twin-arginine translocation pathway

    AU - De Leeuw, Erik

    AU - Porcelli, Ida

    AU - Sargent, Frank

    AU - Palmer, Tracy

    AU - Berks, Ben C

    PY - 2001/10/5

    Y1 - 2001/10/5

    N2 - The Escherichia coli Tat system mediates Sec-independent export of protein precursors bearing twin-arginine signal peptides. The essential Tat pathway components TatA, TatB and TatC are shown to be integral membrane proteins. Upon removal of the predicted N-terminal transmembrane helix TatA becomes a water-soluble protein. In contrast the homologous TatB protein retains weak peripheral interactions with the cytoplasmic membrane when the analogous helix is deleted. Chemical crosslinking studies indicate that TatA forms at least homotrimers, and TatB minimally homodimers, in the native membrane environment. The presence of such homo-oligomeric interactions is supported by size exclusion chromatography. (C) 2001 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.

    AB - The Escherichia coli Tat system mediates Sec-independent export of protein precursors bearing twin-arginine signal peptides. The essential Tat pathway components TatA, TatB and TatC are shown to be integral membrane proteins. Upon removal of the predicted N-terminal transmembrane helix TatA becomes a water-soluble protein. In contrast the homologous TatB protein retains weak peripheral interactions with the cytoplasmic membrane when the analogous helix is deleted. Chemical crosslinking studies indicate that TatA forms at least homotrimers, and TatB minimally homodimers, in the native membrane environment. The presence of such homo-oligomeric interactions is supported by size exclusion chromatography. (C) 2001 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.

    U2 - 10.1016/S0014-5793(01)02904-0

    DO - 10.1016/S0014-5793(01)02904-0

    M3 - Article

    VL - 506

    SP - 143

    EP - 148

    JO - FEBS Letters

    JF - FEBS Letters

    SN - 0014-5793

    IS - 2

    ER -