The Bam complex catalyzes efficient insertion of bacterial outer membrane proteins into membrane vesicles of variable lipid composition [Microbiology]
Sunyia Hussain, Harris D. Bernstein
The American Society for Biochemistry and Molecular Biology (ASBMB)
Published 2018
The American Society for Biochemistry and Molecular Biology (ASBMB)
Published 2018
| Publication Date: |
2018-02-24
|
|---|---|
| Publisher: |
The American Society for Biochemistry and Molecular Biology (ASBMB)
|
| Print ISSN: |
0021-9258
|
| Electronic ISSN: |
1083-351X
|
| Topics: |
Biology
Chemistry and Pharmacology
|
| Published by: |
| _version_ | 1839207918388379648 |
|---|---|
| autor | Sunyia Hussain, Harris D. Bernstein |
| beschreibung | Most proteins that reside in the bacterial outer membrane (OM) have a distinctive “β-barrel” architecture, but the assembly of these proteins is poorly understood. The spontaneous assembly of OM proteins (OMPs) into pure lipid vesicles has been studied extensively but often requires non-physiological conditions and time scales and is strongly influenced by properties of the lipid bilayer, including surface charge, thickness, and fluidity. Furthermore, the membrane insertion of OMPs in vivo is catalyzed by a heterooligomer called the β-barrel assembly machinery (Bam) complex. To determine the role of lipids in the assembly of OMPs under more physiological conditions, we exploited an assay in which the Bam complex mediates their insertion into membrane vesicles. After reconstituting the Bam complex into vesicles that contain a variety of different synthetic lipids, we found that two model OMPs, EspP and OmpA, folded efficiently regardless of the lipid composition. Most notably, both proteins folded into membranes composed of a gel-phase lipid that mimics the rigid bacterial OM. Interestingly, we found that EspP, OmpA, and another model protein (OmpG) folded at significantly different rates and that an α-helix embedded inside the EspP β-barrel accelerates folding. Our results show that the Bam complex largely overcomes effects that lipids exert on OMP assembly and suggest that specific interactions between the Bam complex and an OMP influence its rate of folding. |
| citation_standardnr | 6174192 |
| datenlieferant | ipn_articles |
| feed_id | 43 |
| feed_publisher | The American Society for Biochemistry and Molecular Biology (ASBMB) |
| feed_publisher_url | http://www.asbmb.org/ |
| insertion_date | 2018-02-24 |
| journaleissn | 1083-351X |
| journalissn | 0021-9258 |
| publikationsjahr_anzeige | 2018 |
| publikationsjahr_facette | 2018 |
| publikationsjahr_intervall | 7984:2015-2019 |
| publikationsjahr_sort | 2018 |
| publisher | The American Society for Biochemistry and Molecular Biology (ASBMB) |
| quelle | Journal of Biological Chemistry |
| relation | http://feedproxy.google.com/~r/jbc/SUcv/~3/tsakIiH_SV4/2959.short |
| search_space | articles |
| shingle_author_1 | Sunyia Hussain, Harris D. Bernstein |
| shingle_author_2 | Sunyia Hussain, Harris D. Bernstein |
| shingle_author_3 | Sunyia Hussain, Harris D. Bernstein |
| shingle_author_4 | Sunyia Hussain, Harris D. Bernstein |
| shingle_catch_all_1 | The Bam complex catalyzes efficient insertion of bacterial outer membrane proteins into membrane vesicles of variable lipid composition [Microbiology] Most proteins that reside in the bacterial outer membrane (OM) have a distinctive “β-barrel” architecture, but the assembly of these proteins is poorly understood. The spontaneous assembly of OM proteins (OMPs) into pure lipid vesicles has been studied extensively but often requires non-physiological conditions and time scales and is strongly influenced by properties of the lipid bilayer, including surface charge, thickness, and fluidity. Furthermore, the membrane insertion of OMPs in vivo is catalyzed by a heterooligomer called the β-barrel assembly machinery (Bam) complex. To determine the role of lipids in the assembly of OMPs under more physiological conditions, we exploited an assay in which the Bam complex mediates their insertion into membrane vesicles. After reconstituting the Bam complex into vesicles that contain a variety of different synthetic lipids, we found that two model OMPs, EspP and OmpA, folded efficiently regardless of the lipid composition. Most notably, both proteins folded into membranes composed of a gel-phase lipid that mimics the rigid bacterial OM. Interestingly, we found that EspP, OmpA, and another model protein (OmpG) folded at significantly different rates and that an α-helix embedded inside the EspP β-barrel accelerates folding. Our results show that the Bam complex largely overcomes effects that lipids exert on OMP assembly and suggest that specific interactions between the Bam complex and an OMP influence its rate of folding. Sunyia Hussain, Harris D. Bernstein The American Society for Biochemistry and Molecular Biology (ASBMB) 0021-9258 00219258 1083-351X 1083351X |
| shingle_catch_all_2 | The Bam complex catalyzes efficient insertion of bacterial outer membrane proteins into membrane vesicles of variable lipid composition [Microbiology] Most proteins that reside in the bacterial outer membrane (OM) have a distinctive “β-barrel” architecture, but the assembly of these proteins is poorly understood. The spontaneous assembly of OM proteins (OMPs) into pure lipid vesicles has been studied extensively but often requires non-physiological conditions and time scales and is strongly influenced by properties of the lipid bilayer, including surface charge, thickness, and fluidity. Furthermore, the membrane insertion of OMPs in vivo is catalyzed by a heterooligomer called the β-barrel assembly machinery (Bam) complex. To determine the role of lipids in the assembly of OMPs under more physiological conditions, we exploited an assay in which the Bam complex mediates their insertion into membrane vesicles. After reconstituting the Bam complex into vesicles that contain a variety of different synthetic lipids, we found that two model OMPs, EspP and OmpA, folded efficiently regardless of the lipid composition. Most notably, both proteins folded into membranes composed of a gel-phase lipid that mimics the rigid bacterial OM. Interestingly, we found that EspP, OmpA, and another model protein (OmpG) folded at significantly different rates and that an α-helix embedded inside the EspP β-barrel accelerates folding. Our results show that the Bam complex largely overcomes effects that lipids exert on OMP assembly and suggest that specific interactions between the Bam complex and an OMP influence its rate of folding. Sunyia Hussain, Harris D. Bernstein The American Society for Biochemistry and Molecular Biology (ASBMB) 0021-9258 00219258 1083-351X 1083351X |
| shingle_catch_all_3 | The Bam complex catalyzes efficient insertion of bacterial outer membrane proteins into membrane vesicles of variable lipid composition [Microbiology] Most proteins that reside in the bacterial outer membrane (OM) have a distinctive “β-barrel” architecture, but the assembly of these proteins is poorly understood. The spontaneous assembly of OM proteins (OMPs) into pure lipid vesicles has been studied extensively but often requires non-physiological conditions and time scales and is strongly influenced by properties of the lipid bilayer, including surface charge, thickness, and fluidity. Furthermore, the membrane insertion of OMPs in vivo is catalyzed by a heterooligomer called the β-barrel assembly machinery (Bam) complex. To determine the role of lipids in the assembly of OMPs under more physiological conditions, we exploited an assay in which the Bam complex mediates their insertion into membrane vesicles. After reconstituting the Bam complex into vesicles that contain a variety of different synthetic lipids, we found that two model OMPs, EspP and OmpA, folded efficiently regardless of the lipid composition. Most notably, both proteins folded into membranes composed of a gel-phase lipid that mimics the rigid bacterial OM. Interestingly, we found that EspP, OmpA, and another model protein (OmpG) folded at significantly different rates and that an α-helix embedded inside the EspP β-barrel accelerates folding. Our results show that the Bam complex largely overcomes effects that lipids exert on OMP assembly and suggest that specific interactions between the Bam complex and an OMP influence its rate of folding. Sunyia Hussain, Harris D. Bernstein The American Society for Biochemistry and Molecular Biology (ASBMB) 0021-9258 00219258 1083-351X 1083351X |
| shingle_catch_all_4 | The Bam complex catalyzes efficient insertion of bacterial outer membrane proteins into membrane vesicles of variable lipid composition [Microbiology] Most proteins that reside in the bacterial outer membrane (OM) have a distinctive “β-barrel” architecture, but the assembly of these proteins is poorly understood. The spontaneous assembly of OM proteins (OMPs) into pure lipid vesicles has been studied extensively but often requires non-physiological conditions and time scales and is strongly influenced by properties of the lipid bilayer, including surface charge, thickness, and fluidity. Furthermore, the membrane insertion of OMPs in vivo is catalyzed by a heterooligomer called the β-barrel assembly machinery (Bam) complex. To determine the role of lipids in the assembly of OMPs under more physiological conditions, we exploited an assay in which the Bam complex mediates their insertion into membrane vesicles. After reconstituting the Bam complex into vesicles that contain a variety of different synthetic lipids, we found that two model OMPs, EspP and OmpA, folded efficiently regardless of the lipid composition. Most notably, both proteins folded into membranes composed of a gel-phase lipid that mimics the rigid bacterial OM. Interestingly, we found that EspP, OmpA, and another model protein (OmpG) folded at significantly different rates and that an α-helix embedded inside the EspP β-barrel accelerates folding. Our results show that the Bam complex largely overcomes effects that lipids exert on OMP assembly and suggest that specific interactions between the Bam complex and an OMP influence its rate of folding. Sunyia Hussain, Harris D. Bernstein The American Society for Biochemistry and Molecular Biology (ASBMB) 0021-9258 00219258 1083-351X 1083351X |
| shingle_title_1 | The Bam complex catalyzes efficient insertion of bacterial outer membrane proteins into membrane vesicles of variable lipid composition [Microbiology] |
| shingle_title_2 | The Bam complex catalyzes efficient insertion of bacterial outer membrane proteins into membrane vesicles of variable lipid composition [Microbiology] |
| shingle_title_3 | The Bam complex catalyzes efficient insertion of bacterial outer membrane proteins into membrane vesicles of variable lipid composition [Microbiology] |
| shingle_title_4 | The Bam complex catalyzes efficient insertion of bacterial outer membrane proteins into membrane vesicles of variable lipid composition [Microbiology] |
| timestamp | 2025-07-31T23:42:34.234Z |
| titel | The Bam complex catalyzes efficient insertion of bacterial outer membrane proteins into membrane vesicles of variable lipid composition [Microbiology] |
| titel_suche | The Bam complex catalyzes efficient insertion of bacterial outer membrane proteins into membrane vesicles of variable lipid composition [Microbiology] |
| topic | W V |
| uid | ipn_articles_6174192 |