TY - CHAP
T1 - The β-barrel assembly machinery complex
AU - Leyton, Denisse L.
AU - Belousoff, Matthew J.
AU - Lithgow, Trevor
N1 - Publisher Copyright:
© Springer Science+Business Media New York 2015.
PY - 2015/4/1
Y1 - 2015/4/1
N2 - The outer membranes of gram-negative bacteria contain integral membrane proteins, most of which are of β-barrel structure, and critical for bacterial survival. These β-barrel proteins rely on the β -barrel a ssembly m achinery (BAM) complex for their integration into the outer membrane as folded species. The central and essential subunit of the BAM complex, BamA, is a β-barrel protein conserved in all gram-negative bacteria and also found in eukaryotic organelles derived from bacterial endosymbionts. In Escherichia coli, BamA docks with four peripheral lipoproteins, BamB, BamC, BamD and BamE, partner subunits that add to the function of the BAM complex in outer membrane protein biogenesis. By way of introduction to this volume, we provide an overview of the work that has illuminated the mechanism by which the BAM complex drives β-barrel assembly. The protocols and methodologies associated with these studies as well as the challenges encountered and their elegant solutions are discussed in subsequent chapters.
AB - The outer membranes of gram-negative bacteria contain integral membrane proteins, most of which are of β-barrel structure, and critical for bacterial survival. These β-barrel proteins rely on the β -barrel a ssembly m achinery (BAM) complex for their integration into the outer membrane as folded species. The central and essential subunit of the BAM complex, BamA, is a β-barrel protein conserved in all gram-negative bacteria and also found in eukaryotic organelles derived from bacterial endosymbionts. In Escherichia coli, BamA docks with four peripheral lipoproteins, BamB, BamC, BamD and BamE, partner subunits that add to the function of the BAM complex in outer membrane protein biogenesis. By way of introduction to this volume, we provide an overview of the work that has illuminated the mechanism by which the BAM complex drives β-barrel assembly. The protocols and methodologies associated with these studies as well as the challenges encountered and their elegant solutions are discussed in subsequent chapters.
KW - BamA
KW - Omp85
KW - Outer membrane
KW - Outer membrane β-barrel proteins (OMPs)
KW - Periplasmic chaperones
KW - β-barrel
KW - β-barrel assembly machinery (BAM)
UR - http://www.scopus.com/inward/record.url?scp=84943327746&partnerID=8YFLogxK
U2 - 10.1007/978-1-4939-2871-2_1
DO - 10.1007/978-1-4939-2871-2_1
M3 - Chapter
T3 - Methods in Molecular Biology
BT - Methods in Molecular Biology
PB - Humana Press Inc.
ER -