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The SDBC is active in quenching oxidative conditions and bridges the cell envelope layers in Deinococcus radiodurans
Deinococcus radiodurans is known for its remarkable ability to withstand harsh stressful conditions. The outermost layer of its cell envelope is a proteinaceous coat, the S-layer, essential for resistance to and interactions with the environment. The S-layer Deinoxanthin-binding complex (SDBC), one...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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American Society for Biochemistry and Molecular Biology
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9823218/ https://www.ncbi.nlm.nih.gov/pubmed/36502921 http://dx.doi.org/10.1016/j.jbc.2022.102784 |
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author | Farci, Domenica Graça, André T. Iesu, Luca de Sanctis, Daniele Piano, Dario |
author_facet | Farci, Domenica Graça, André T. Iesu, Luca de Sanctis, Daniele Piano, Dario |
author_sort | Farci, Domenica |
collection | PubMed |
description | Deinococcus radiodurans is known for its remarkable ability to withstand harsh stressful conditions. The outermost layer of its cell envelope is a proteinaceous coat, the S-layer, essential for resistance to and interactions with the environment. The S-layer Deinoxanthin-binding complex (SDBC), one of the main units of the characteristic multilayered cell envelope of this bacterium, protects against environmental stressors and allows exchanges with the environment. So far, specific regions of this complex, the collar and the stalk, remained unassigned. Here, these regions are resolved by cryo-EM and locally refined. The resulting 3D map shows that the collar region of this multiprotein complex is a trimer of the protein DR_0644, a Cu-only superoxide dismutase (SOD) identified here to be efficient in quenching reactive oxygen species. The same data also showed that the stalk region consists of a coiled coil that extends into the cell envelope for ∼280 Å, reaching the inner membrane. Finally, the orientation and localization of the complex are defined by in situ cryo-electron crystallography. The structural organization of the SDBC couples fundamental UV antenna properties with the presence of a Cu-only SOD, showing here coexisting photoprotective and chemoprotective functions. These features suggests how the SDBC and similar protein complexes, might have played a primary role as evolutive templates for the origin of photoautotrophic processes by combining primary protective needs with more independent energetic strategies. |
format | Online Article Text |
id | pubmed-9823218 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | American Society for Biochemistry and Molecular Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-98232182023-01-09 The SDBC is active in quenching oxidative conditions and bridges the cell envelope layers in Deinococcus radiodurans Farci, Domenica Graça, André T. Iesu, Luca de Sanctis, Daniele Piano, Dario J Biol Chem JBC Communication Deinococcus radiodurans is known for its remarkable ability to withstand harsh stressful conditions. The outermost layer of its cell envelope is a proteinaceous coat, the S-layer, essential for resistance to and interactions with the environment. The S-layer Deinoxanthin-binding complex (SDBC), one of the main units of the characteristic multilayered cell envelope of this bacterium, protects against environmental stressors and allows exchanges with the environment. So far, specific regions of this complex, the collar and the stalk, remained unassigned. Here, these regions are resolved by cryo-EM and locally refined. The resulting 3D map shows that the collar region of this multiprotein complex is a trimer of the protein DR_0644, a Cu-only superoxide dismutase (SOD) identified here to be efficient in quenching reactive oxygen species. The same data also showed that the stalk region consists of a coiled coil that extends into the cell envelope for ∼280 Å, reaching the inner membrane. Finally, the orientation and localization of the complex are defined by in situ cryo-electron crystallography. The structural organization of the SDBC couples fundamental UV antenna properties with the presence of a Cu-only SOD, showing here coexisting photoprotective and chemoprotective functions. These features suggests how the SDBC and similar protein complexes, might have played a primary role as evolutive templates for the origin of photoautotrophic processes by combining primary protective needs with more independent energetic strategies. American Society for Biochemistry and Molecular Biology 2022-12-09 /pmc/articles/PMC9823218/ /pubmed/36502921 http://dx.doi.org/10.1016/j.jbc.2022.102784 Text en © 2022 The Authors https://creativecommons.org/licenses/by/4.0/This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | JBC Communication Farci, Domenica Graça, André T. Iesu, Luca de Sanctis, Daniele Piano, Dario The SDBC is active in quenching oxidative conditions and bridges the cell envelope layers in Deinococcus radiodurans |
title | The SDBC is active in quenching oxidative conditions and bridges the cell envelope layers in Deinococcus radiodurans |
title_full | The SDBC is active in quenching oxidative conditions and bridges the cell envelope layers in Deinococcus radiodurans |
title_fullStr | The SDBC is active in quenching oxidative conditions and bridges the cell envelope layers in Deinococcus radiodurans |
title_full_unstemmed | The SDBC is active in quenching oxidative conditions and bridges the cell envelope layers in Deinococcus radiodurans |
title_short | The SDBC is active in quenching oxidative conditions and bridges the cell envelope layers in Deinococcus radiodurans |
title_sort | sdbc is active in quenching oxidative conditions and bridges the cell envelope layers in deinococcus radiodurans |
topic | JBC Communication |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9823218/ https://www.ncbi.nlm.nih.gov/pubmed/36502921 http://dx.doi.org/10.1016/j.jbc.2022.102784 |
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