scholarly journals Structural basis of outer membrane protein insertion by the BAM complex

Nature ◽  
2016 ◽  
Vol 531 (7592) ◽  
pp. 64-69 ◽  
Author(s):  
Yinghong Gu ◽  
Huanyu Li ◽  
Haohao Dong ◽  
Yi Zeng ◽  
Zhengyu Zhang ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Outer Membrane ◽  
Outer Membrane Protein ◽  
Structural Basis ◽  
Protein Insertion ◽  
Bam Complex ◽  
Membrane Protein Insertion

Structural basis of Sec-independent membrane protein insertion by YidC

Nature ◽  
2014 ◽  
Vol 509 (7501) ◽  
pp. 516-520 ◽  
Author(s):  
Kaoru Kumazaki ◽  
Shinobu Chiba ◽  
Mizuki Takemoto ◽  
Arata Furukawa ◽  
Ken-ichi Nishiyama ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Structural Basis ◽  
Protein Insertion ◽  
Membrane Protein Insertion

scholarly journals Distinctive Roles for Periplasmic Proteases in the Maintenance of Essential Outer Membrane Protein Assembly

2017 ◽  
Vol 199 (20) ◽  
Author(s):  
Garner R. Soltes ◽  
Nicholas R. Martin ◽  
Eunhae Park ◽  
Holly A. Sutterlin ◽  
Thomas J. Silhavy
Keyword(s):  
Quality Control ◽  
Membrane Protein ◽  
Outer Membrane ◽  
Outer Membrane Protein ◽  
Permeability Barrier ◽  
Initial Contact ◽  
Assembly Process ◽  
Intrinsic Resistance ◽  
Control Factors ◽  
Bam Complex

ABSTRACT Outer membrane protein (OMP) biogenesis in Escherichia coli is a robust process essential to the life of the organism. It is catalyzed by the β-barrel assembly machine (Bam) complex, and a number of quality control factors, including periplasmic chaperones and proteases, maintain the integrity of this trafficking pathway. Little is known, however, about how periplasmic proteases recognize and degrade OMP substrates when assembly is compromised or whether different proteases recognize the same substrate at distinct points in the assembly pathway. In this work, we use well-defined assembly-defective mutants of LptD, the essential lipopolysaccharide assembly translocon, to show that the periplasmic protease DegP degrades substrates with assembly defects that prevent or impair initial contact with Bam, causing the mutant protein to accumulate in the periplasm. In contrast, another periplasmic protease, BepA, degrades a LptD mutant substrate that has engaged the Bam complex and formed a nearly complete barrel. Furthermore, we describe the role of the outer membrane lipoprotein YcaL, a protease of heretofore unknown function, in the degradation of a LptD substrate that has engaged the Bam complex but is stalled at an earlier step in the assembly process that is not accessible to BepA. Our results demonstrate that multiple periplasmic proteases monitor OMPs at distinct points in the assembly process. IMPORTANCE OMP assembly is catalyzed by the essential Bam complex and occurs in a cellular environment devoid of energy sources. Assembly intermediates that misfold can compromise this essential molecular machine. Here we demonstrate distinctive roles for three different periplasmic proteases that can clear OMP substrates with folding defects that compromise assembly at three different stages. These quality control factors help ensure the integrity of the permeability barrier that contributes to the intrinsic resistance of Gram-negative organisms to many antibiotics.

scholarly journals Structural Basis for the Interaction of Lipopolysaccharide with Outer Membrane Protein H (OprH) fromPseudomonas aeruginosa

2011 ◽  
Vol 286 (45) ◽  
pp. 39211-39223 ◽  
Author(s):  
Thomas C. Edrington ◽  
Erica Kintz ◽  
Joanna B. Goldberg ◽  
Lukas K. Tamm
Keyword(s):  
Membrane Protein ◽  
Outer Membrane ◽  
Outer Membrane Protein ◽  
Structural Basis
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