A lipoprotein/β-barrel complex monitors lipopolysaccharide integrity transducing information across the outer membrane
Lipoprotein RcsF is the OM component of the Rcs envelope stress response. RcsF exists in complexes with β-barrel proteins (OMPs) allowing it to adopt a transmembrane orientation with a lipidated N-terminal domain on the cell surface and a periplasmic C-terminal domain. Here we report that mutations...
| Main Authors: | , , |
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| Format: | Article |
| Language: | English |
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eLife Sciences Publications Ltd
2016-06-01
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| Series: | eLife |
| Subjects: | |
| Online Access: | https://elifesciences.org/articles/15276 |
| _version_ | 1811180619534696448 |
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| author | Anna Konovalova Angela M Mitchell Thomas J Silhavy |
| author_facet | Anna Konovalova Angela M Mitchell Thomas J Silhavy |
| author_sort | Anna Konovalova |
| collection | DOAJ |
| description | Lipoprotein RcsF is the OM component of the Rcs envelope stress response. RcsF exists in complexes with β-barrel proteins (OMPs) allowing it to adopt a transmembrane orientation with a lipidated N-terminal domain on the cell surface and a periplasmic C-terminal domain. Here we report that mutations that remove BamE or alter a residue in the RcsF trans-lumen domain specifically prevent assembly of the interlocked complexes without inactivating either RcsF or the OMP. Using these mutations we demonstrate that these RcsF/OMP complexes are required for sensing OM outer leaflet stress. Using mutations that alter the positively charged surface-exposed domain, we show that RcsF monitors lateral interactions between lipopolysaccharide (LPS) molecules. When these interactions are disrupted by cationic antimicrobial peptides, or by the loss of negatively charged phosphate groups on the LPS molecule, this information is transduced to the RcsF C-terminal signaling domain located in the periplasm to activate the stress response. |
| first_indexed | 2024-04-11T09:06:17Z |
| format | Article |
| id | doaj.art-834ce531e7524653baca43f47d050b4b |
| institution | Directory Open Access Journal |
| issn | 2050-084X |
| language | English |
| last_indexed | 2024-04-11T09:06:17Z |
| publishDate | 2016-06-01 |
| publisher | eLife Sciences Publications Ltd |
| record_format | Article |
| series | eLife |
| spelling | doaj.art-834ce531e7524653baca43f47d050b4b2022-12-22T04:32:37ZengeLife Sciences Publications LtdeLife2050-084X2016-06-01510.7554/eLife.15276A lipoprotein/β-barrel complex monitors lipopolysaccharide integrity transducing information across the outer membraneAnna Konovalova0https://orcid.org/0000-0002-2238-8849Angela M Mitchell1Thomas J Silhavy2https://orcid.org/0000-0001-7672-5153Department of Molecular Biology, Princeton University, Lewis Thomas Laboratory, Princeton, United StatesDepartment of Molecular Biology, Princeton University, Lewis Thomas Laboratory, Princeton, United StatesDepartment of Molecular Biology, Princeton University, Lewis Thomas Laboratory, Princeton, United StatesLipoprotein RcsF is the OM component of the Rcs envelope stress response. RcsF exists in complexes with β-barrel proteins (OMPs) allowing it to adopt a transmembrane orientation with a lipidated N-terminal domain on the cell surface and a periplasmic C-terminal domain. Here we report that mutations that remove BamE or alter a residue in the RcsF trans-lumen domain specifically prevent assembly of the interlocked complexes without inactivating either RcsF or the OMP. Using these mutations we demonstrate that these RcsF/OMP complexes are required for sensing OM outer leaflet stress. Using mutations that alter the positively charged surface-exposed domain, we show that RcsF monitors lateral interactions between lipopolysaccharide (LPS) molecules. When these interactions are disrupted by cationic antimicrobial peptides, or by the loss of negatively charged phosphate groups on the LPS molecule, this information is transduced to the RcsF C-terminal signaling domain located in the periplasm to activate the stress response.https://elifesciences.org/articles/15276signal transductionBam complexpolymyxin Bsurface exposed lipoproteinmembrane biogenesisCAMP |
| spellingShingle | Anna Konovalova Angela M Mitchell Thomas J Silhavy A lipoprotein/β-barrel complex monitors lipopolysaccharide integrity transducing information across the outer membrane eLife signal transduction Bam complex polymyxin B surface exposed lipoprotein membrane biogenesis CAMP |
| title | A lipoprotein/β-barrel complex monitors lipopolysaccharide integrity transducing information across the outer membrane |
| title_full | A lipoprotein/β-barrel complex monitors lipopolysaccharide integrity transducing information across the outer membrane |
| title_fullStr | A lipoprotein/β-barrel complex monitors lipopolysaccharide integrity transducing information across the outer membrane |
| title_full_unstemmed | A lipoprotein/β-barrel complex monitors lipopolysaccharide integrity transducing information across the outer membrane |
| title_short | A lipoprotein/β-barrel complex monitors lipopolysaccharide integrity transducing information across the outer membrane |
| title_sort | lipoprotein β barrel complex monitors lipopolysaccharide integrity transducing information across the outer membrane |
| topic | signal transduction Bam complex polymyxin B surface exposed lipoprotein membrane biogenesis CAMP |
| url | https://elifesciences.org/articles/15276 |
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