Transport and proofreading of proteins by the twin-arginine translocation (Tat) system in bacteria

Colin Robinson, Cristina F R O Matos, Daniel Beck, Chao Ren, Janna Lawrence, Nishi Vasisht, Sharon Mendel

    Research output: Contribution to journalArticle

    70 Citations (Scopus)

    Abstract

    The twin-arginine translocation (Tat) system operates in plant thylakoid membranes and the plasma membranes of most free-living bacteria. In bacteria, it is responsible for the export of a number of proteins to the periplasm, outer membrane or growth medium, selecting substrates by virtue of cleavable N-terminal signal peptides that contain a key twin-arginine motif together with other determinants. Its most notable attribute is its ability to transport large folded proteins (even oligomeric proteins) across the tightly sealed plasma membrane. In Gram-negative bacteria, TatABC subunits appear to carry out all of the essential translocation functions in the form of two distinct complexes at steady state: a TatABC substrate-binding complex and separate TatA complex. Several studies favour a model in which these complexes transiently coalesce to generate the full translocase. Most Gram-positive organisms possess an even simpler "minimalist" Tat system which lacks a TatB component and contains, instead, a bifunctional TatA component. These Tat systems may involve the operation of a TatAC complex together with a separate TatA complex, although a radically different model for TatAC-type systems has also been proposed. While bacterial Tat systems appear to require the presence of only a few proteins for the actual translocation event, there is increasing evidence for the operation of ancillary components that carry out sophisticated "proofreading" activities. These activities ensure that redox proteins are only exported after full assembly of the cofactor, thereby avoiding the futile export of apo-forms. This article is part of a Special Issue entitled Protein translocation across or insertion into membranes.

    Original languageEnglish
    Pages (from-to)876-884
    Number of pages9
    JournalBiochimica et biophysica acta
    Volume1808
    Issue number3
    DOIs
    Publication statusPublished - Mar 2011

    Fingerprint

    Carrier Proteins
    Bacteria
    Protein Transport
    Proteins
    Cell Membrane
    Periplasm
    Thylakoids
    Membranes
    Protein Sorting Signals
    Gram-Negative Bacteria
    Oxidation-Reduction
    Arginine
    Twin-Arginine-Translocation System
    Growth

    Keywords

    • Amino Acid Sequence
    • Arginine
    • Biological Transport
    • Escherichia coli
    • Escherichia coli Proteins
    • Membrane Transport Proteins
    • Molecular Sequence Data
    • Protein Sorting Signals
    • Protein Transport
    • Sequence Homology, Amino Acid
    • Journal Article
    • Review

    Cite this

    Transport and proofreading of proteins by the twin-arginine translocation (Tat) system in bacteria. / Robinson, Colin; Matos, Cristina F R O; Beck, Daniel; Ren, Chao; Lawrence, Janna; Vasisht, Nishi; Mendel, Sharon.

    In: Biochimica et biophysica acta, Vol. 1808, No. 3, 03.2011, p. 876-884.

    Research output: Contribution to journalArticle

    Robinson, Colin ; Matos, Cristina F R O ; Beck, Daniel ; Ren, Chao ; Lawrence, Janna ; Vasisht, Nishi ; Mendel, Sharon. / Transport and proofreading of proteins by the twin-arginine translocation (Tat) system in bacteria. In: Biochimica et biophysica acta. 2011 ; Vol. 1808, No. 3. pp. 876-884.
    @article{de859d84e3bd4fc893e2523cf86c217c,
    title = "Transport and proofreading of proteins by the twin-arginine translocation (Tat) system in bacteria",
    abstract = "The twin-arginine translocation (Tat) system operates in plant thylakoid membranes and the plasma membranes of most free-living bacteria. In bacteria, it is responsible for the export of a number of proteins to the periplasm, outer membrane or growth medium, selecting substrates by virtue of cleavable N-terminal signal peptides that contain a key twin-arginine motif together with other determinants. Its most notable attribute is its ability to transport large folded proteins (even oligomeric proteins) across the tightly sealed plasma membrane. In Gram-negative bacteria, TatABC subunits appear to carry out all of the essential translocation functions in the form of two distinct complexes at steady state: a TatABC substrate-binding complex and separate TatA complex. Several studies favour a model in which these complexes transiently coalesce to generate the full translocase. Most Gram-positive organisms possess an even simpler {"}minimalist{"} Tat system which lacks a TatB component and contains, instead, a bifunctional TatA component. These Tat systems may involve the operation of a TatAC complex together with a separate TatA complex, although a radically different model for TatAC-type systems has also been proposed. While bacterial Tat systems appear to require the presence of only a few proteins for the actual translocation event, there is increasing evidence for the operation of ancillary components that carry out sophisticated {"}proofreading{"} activities. These activities ensure that redox proteins are only exported after full assembly of the cofactor, thereby avoiding the futile export of apo-forms. This article is part of a Special Issue entitled Protein translocation across or insertion into membranes.",
    keywords = "Amino Acid Sequence, Arginine, Biological Transport, Escherichia coli, Escherichia coli Proteins, Membrane Transport Proteins, Molecular Sequence Data, Protein Sorting Signals, Protein Transport, Sequence Homology, Amino Acid, Journal Article, Review",
    author = "Colin Robinson and Matos, {Cristina F R O} and Daniel Beck and Chao Ren and Janna Lawrence and Nishi Vasisht and Sharon Mendel",
    note = "Copyright {\circledC} 2011 Elsevier B.V. All rights reserved.",
    year = "2011",
    month = "3",
    doi = "10.1016/j.bbamem.2010.11.023",
    language = "English",
    volume = "1808",
    pages = "876--884",
    journal = "Biochimica et biophysica acta",
    issn = "0006-3002",
    publisher = "Elsevier",
    number = "3",

    }

    TY - JOUR

    T1 - Transport and proofreading of proteins by the twin-arginine translocation (Tat) system in bacteria

    AU - Robinson, Colin

    AU - Matos, Cristina F R O

    AU - Beck, Daniel

    AU - Ren, Chao

    AU - Lawrence, Janna

    AU - Vasisht, Nishi

    AU - Mendel, Sharon

    N1 - Copyright © 2011 Elsevier B.V. All rights reserved.

    PY - 2011/3

    Y1 - 2011/3

    N2 - The twin-arginine translocation (Tat) system operates in plant thylakoid membranes and the plasma membranes of most free-living bacteria. In bacteria, it is responsible for the export of a number of proteins to the periplasm, outer membrane or growth medium, selecting substrates by virtue of cleavable N-terminal signal peptides that contain a key twin-arginine motif together with other determinants. Its most notable attribute is its ability to transport large folded proteins (even oligomeric proteins) across the tightly sealed plasma membrane. In Gram-negative bacteria, TatABC subunits appear to carry out all of the essential translocation functions in the form of two distinct complexes at steady state: a TatABC substrate-binding complex and separate TatA complex. Several studies favour a model in which these complexes transiently coalesce to generate the full translocase. Most Gram-positive organisms possess an even simpler "minimalist" Tat system which lacks a TatB component and contains, instead, a bifunctional TatA component. These Tat systems may involve the operation of a TatAC complex together with a separate TatA complex, although a radically different model for TatAC-type systems has also been proposed. While bacterial Tat systems appear to require the presence of only a few proteins for the actual translocation event, there is increasing evidence for the operation of ancillary components that carry out sophisticated "proofreading" activities. These activities ensure that redox proteins are only exported after full assembly of the cofactor, thereby avoiding the futile export of apo-forms. This article is part of a Special Issue entitled Protein translocation across or insertion into membranes.

    AB - The twin-arginine translocation (Tat) system operates in plant thylakoid membranes and the plasma membranes of most free-living bacteria. In bacteria, it is responsible for the export of a number of proteins to the periplasm, outer membrane or growth medium, selecting substrates by virtue of cleavable N-terminal signal peptides that contain a key twin-arginine motif together with other determinants. Its most notable attribute is its ability to transport large folded proteins (even oligomeric proteins) across the tightly sealed plasma membrane. In Gram-negative bacteria, TatABC subunits appear to carry out all of the essential translocation functions in the form of two distinct complexes at steady state: a TatABC substrate-binding complex and separate TatA complex. Several studies favour a model in which these complexes transiently coalesce to generate the full translocase. Most Gram-positive organisms possess an even simpler "minimalist" Tat system which lacks a TatB component and contains, instead, a bifunctional TatA component. These Tat systems may involve the operation of a TatAC complex together with a separate TatA complex, although a radically different model for TatAC-type systems has also been proposed. While bacterial Tat systems appear to require the presence of only a few proteins for the actual translocation event, there is increasing evidence for the operation of ancillary components that carry out sophisticated "proofreading" activities. These activities ensure that redox proteins are only exported after full assembly of the cofactor, thereby avoiding the futile export of apo-forms. This article is part of a Special Issue entitled Protein translocation across or insertion into membranes.

    KW - Amino Acid Sequence

    KW - Arginine

    KW - Biological Transport

    KW - Escherichia coli

    KW - Escherichia coli Proteins

    KW - Membrane Transport Proteins

    KW - Molecular Sequence Data

    KW - Protein Sorting Signals

    KW - Protein Transport

    KW - Sequence Homology, Amino Acid

    KW - Journal Article

    KW - Review

    U2 - 10.1016/j.bbamem.2010.11.023

    DO - 10.1016/j.bbamem.2010.11.023

    M3 - Article

    VL - 1808

    SP - 876

    EP - 884

    JO - Biochimica et biophysica acta

    JF - Biochimica et biophysica acta

    SN - 0006-3002

    IS - 3

    ER -