The TAM: A translocation and assembly module of the β-barrel assembly machinery in bacterial outer membranes

Christopher J. Stubenrauch; Trevor Lithgow

doi:10.1128/9781683670285.ch9

The TAM: A translocation and assembly module of the β-barrel assembly machinery in bacterial outer membranes

Christopher J. Stubenrauch, Trevor Lithgow

Research output: Chapter in Book/Report/Conference proceeding › Chapter (Book) › Other › peer-review

1 Citation (Scopus)

Abstract

The vast majority of integral membrane proteins residing within the outer membrane of Gram-negative bacteria adopt a β-barrel architecture. Mechanistically, how these proteins fold remains uncertain, but the process requires assistance from at least two nanomachines: the translocation and assembly module (TAM) and the β-barrel assembly machinery (BAM) complex (^1-3). But whether the TAM and the BAM complex collaborate or act independently on each nascent membrane protein substrate arriving at the outer membrane has yet to be determined. The TAM is comprised of two subunits: TamA, an integral outer membrane protein (^{2, 4, 5}), and TamB, an inner membrane-anchored protein (²). The BAM complex is variable in composition between genera, and it is comprised of 2 to 5 accessory lipoproteins attached to an integral outer membrane protein, BamA (^{1, 6, 7}).

Original language	English
Title of host publication	Protein Secretion in Bacteria
Editors	Maria Sandkvist, Eric Cascales, Peter J. Christie
Place of Publication	Washington, DC, USA
Publisher	Wiley-Academy
Chapter	9
Pages	103-111
Number of pages	9
ISBN (Electronic)	9781683670445
ISBN (Print)	9781683670278
DOIs	https://doi.org/10.1128/9781683670285.ch9
Publication status	Published - 1 Jan 2019

Keywords

Bacterial outer membranes
Crystal structure
Gating mechanism
Polypeptide transport-associated domains
Translocation and assembly module
β-barrel assembly machinery

Access to Document

10.1128/9781683670285.ch9

Cite this

@inbook{c2edc343b05b48278fef0467650f46a6,

title = "The TAM: A translocation and assembly module of the β-barrel assembly machinery in bacterial outer membranes",

abstract = "The vast majority of integral membrane proteins residing within the outer membrane of Gram-negative bacteria adopt a β-barrel architecture. Mechanistically, how these proteins fold remains uncertain, but the process requires assistance from at least two nanomachines: the translocation and assembly module (TAM) and the β-barrel assembly machinery (BAM) complex (1-3). But whether the TAM and the BAM complex collaborate or act independently on each nascent membrane protein substrate arriving at the outer membrane has yet to be determined. The TAM is comprised of two subunits: TamA, an integral outer membrane protein (2, 4, 5), and TamB, an inner membrane-anchored protein (2). The BAM complex is variable in composition between genera, and it is comprised of 2 to 5 accessory lipoproteins attached to an integral outer membrane protein, BamA (1, 6, 7).",

keywords = "Bacterial outer membranes, Crystal structure, Gating mechanism, Polypeptide transport-associated domains, Translocation and assembly module, β-barrel assembly machinery",

author = "Stubenrauch, {Christopher J.} and Trevor Lithgow",

note = "This work was published as part of a larger work (in book chapter format) and was also published as a stand-alone review in the journal EcoSal Plus. There are no differences between the two published versions. Publisher Copyright: {\textcopyright} 2019 American Society for Microbiology.",

year = "2019",

month = jan,

day = "1",

doi = "10.1128/9781683670285.ch9",

language = "English",

isbn = "9781683670278",

pages = "103--111",

editor = "Maria Sandkvist and Eric Cascales and Christie, {Peter J.}",

booktitle = "Protein Secretion in Bacteria",

publisher = "Wiley-Academy",

}

The TAM: A translocation and assembly module of the β-barrel assembly machinery in bacterial outer membranes. / Stubenrauch, Christopher J.; Lithgow, Trevor.
Protein Secretion in Bacteria. ed. / Maria Sandkvist; Eric Cascales; Peter J. Christie. Washington, DC, USA: Wiley-Academy, 2019. p. 103-111.

Research output: Chapter in Book/Report/Conference proceeding › Chapter (Book) › Other › peer-review

TY - CHAP

T1 - The TAM

T2 - A translocation and assembly module of the β-barrel assembly machinery in bacterial outer membranes

AU - Stubenrauch, Christopher J.

AU - Lithgow, Trevor

N1 - This work was published as part of a larger work (in book chapter format) and was also published as a stand-alone review in the journal EcoSal Plus. There are no differences between the two published versions. Publisher Copyright: © 2019 American Society for Microbiology.

PY - 2019/1/1

Y1 - 2019/1/1

N2 - The vast majority of integral membrane proteins residing within the outer membrane of Gram-negative bacteria adopt a β-barrel architecture. Mechanistically, how these proteins fold remains uncertain, but the process requires assistance from at least two nanomachines: the translocation and assembly module (TAM) and the β-barrel assembly machinery (BAM) complex (1-3). But whether the TAM and the BAM complex collaborate or act independently on each nascent membrane protein substrate arriving at the outer membrane has yet to be determined. The TAM is comprised of two subunits: TamA, an integral outer membrane protein (2, 4, 5), and TamB, an inner membrane-anchored protein (2). The BAM complex is variable in composition between genera, and it is comprised of 2 to 5 accessory lipoproteins attached to an integral outer membrane protein, BamA (1, 6, 7).

AB - The vast majority of integral membrane proteins residing within the outer membrane of Gram-negative bacteria adopt a β-barrel architecture. Mechanistically, how these proteins fold remains uncertain, but the process requires assistance from at least two nanomachines: the translocation and assembly module (TAM) and the β-barrel assembly machinery (BAM) complex (1-3). But whether the TAM and the BAM complex collaborate or act independently on each nascent membrane protein substrate arriving at the outer membrane has yet to be determined. The TAM is comprised of two subunits: TamA, an integral outer membrane protein (2, 4, 5), and TamB, an inner membrane-anchored protein (2). The BAM complex is variable in composition between genera, and it is comprised of 2 to 5 accessory lipoproteins attached to an integral outer membrane protein, BamA (1, 6, 7).

KW - Bacterial outer membranes

KW - Crystal structure

KW - Gating mechanism

KW - Polypeptide transport-associated domains

KW - Translocation and assembly module

KW - β-barrel assembly machinery

UR - http://www.scopus.com/inward/record.url?scp=85140940387&partnerID=8YFLogxK

U2 - 10.1128/9781683670285.ch9

DO - 10.1128/9781683670285.ch9

M3 - Chapter (Book)

AN - SCOPUS:85140940387

SN - 9781683670278

SP - 103

EP - 111

BT - Protein Secretion in Bacteria

A2 - Sandkvist, Maria

A2 - Cascales, Eric

A2 - Christie, Peter J.

PB - Wiley-Academy

CY - Washington, DC, USA

ER -

The TAM: A translocation and assembly module of the β-barrel assembly machinery in bacterial outer membranes

Abstract

Keywords

Access to Document

Other files and links