Interplay between DsbA1, DsbA2 and C8J_1298 Periplasmic Oxidoreductases of <i>Campylobacter jejuni</i> and Their Impact on Bacterial Physiology and Pathogenesis
The bacterial proteins of the Dsb family catalyze the formation of disulfide bridges between cysteine residues that stabilize protein structures and ensure their proper functioning. Here, we report the detailed analysis of the Dsb pathway of <i>Campylobacter jejuni</i>. The oxidizing Dsb...
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2021-12-01
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| Series: | International Journal of Molecular Sciences |
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| Online Access: | https://www.mdpi.com/1422-0067/22/24/13451 |
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| author | Anna M. Banaś Katarzyna M. Bocian-Ostrzycka Stanisław Dunin-Horkawicz Jan Ludwiczak Piotr Wilk Marta Orlikowska Agnieszka Wyszyńska Maria Dąbrowska Maciej Plichta Marta Spodzieja Marta A. Polańska Agata Malinowska Elżbieta Katarzyna Jagusztyn-Krynicka |
| author_facet | Anna M. Banaś Katarzyna M. Bocian-Ostrzycka Stanisław Dunin-Horkawicz Jan Ludwiczak Piotr Wilk Marta Orlikowska Agnieszka Wyszyńska Maria Dąbrowska Maciej Plichta Marta Spodzieja Marta A. Polańska Agata Malinowska Elżbieta Katarzyna Jagusztyn-Krynicka |
| author_sort | Anna M. Banaś |
| collection | DOAJ |
| description | The bacterial proteins of the Dsb family catalyze the formation of disulfide bridges between cysteine residues that stabilize protein structures and ensure their proper functioning. Here, we report the detailed analysis of the Dsb pathway of <i>Campylobacter jejuni</i>. The oxidizing Dsb system of this pathogen is unique because it consists of two monomeric DsbAs (DsbA1 and DsbA2) and one dimeric bifunctional protein (C8J_1298). Previously, we showed that DsbA1 and C8J_1298 are redundant. Here, we unraveled the interaction between the two monomeric DsbAs by in vitro and in vivo experiments and by solving their structures and found that both monomeric DsbAs are dispensable proteins. Their structures confirmed that they are homologs of EcDsbL. The slight differences seen in the surface charge of the proteins do not affect the interaction with their redox partner. Comparative proteomics showed that several respiratory proteins, as well as periplasmic transport proteins, are targets of the Dsb system. Some of these, both donors and electron acceptors, are essential elements of the <i>C. jejuni</i> respiratory process under oxygen-limiting conditions in the host intestine. The data presented provide detailed information on the function of the <i>C. jejuni</i> Dsb system, identifying it as a potential target for novel antibacterial molecules. |
| first_indexed | 2024-03-10T03:55:32Z |
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| institution | Directory Open Access Journal |
| issn | 1661-6596 1422-0067 |
| language | English |
| last_indexed | 2024-03-10T03:55:32Z |
| publishDate | 2021-12-01 |
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| series | International Journal of Molecular Sciences |
| spelling | doaj.art-547c04ddddb8441fb0979aae7e45e0952023-11-23T08:46:33ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672021-12-0122241345110.3390/ijms222413451Interplay between DsbA1, DsbA2 and C8J_1298 Periplasmic Oxidoreductases of <i>Campylobacter jejuni</i> and Their Impact on Bacterial Physiology and PathogenesisAnna M. Banaś0Katarzyna M. Bocian-Ostrzycka1Stanisław Dunin-Horkawicz2Jan Ludwiczak3Piotr Wilk4Marta Orlikowska5Agnieszka Wyszyńska6Maria Dąbrowska7Maciej Plichta8Marta Spodzieja9Marta A. Polańska10Agata Malinowska11Elżbieta Katarzyna Jagusztyn-Krynicka12Department of Bacterial Genetics, Faculty of Biology, Institute of Microbiology, University of Warsaw, 02-096 Warsaw, PolandDepartment of Bacterial Genetics, Faculty of Biology, Institute of Microbiology, University of Warsaw, 02-096 Warsaw, PolandLaboratory of Structural Bioinformatics, Centre of New Technologies, University of Warsaw, 02-097 Warsaw, PolandLaboratory of Structural Bioinformatics, Centre of New Technologies, University of Warsaw, 02-097 Warsaw, PolandMalopolska Centre of Biotechnology, Jagiellonian University, 30-387 Cracow, PolandFaculty of Chemistry, University of Gdańsk, 80-308 Gdansk, PolandDepartment of Bacterial Genetics, Faculty of Biology, Institute of Microbiology, University of Warsaw, 02-096 Warsaw, PolandDepartment of Bacterial Genetics, Faculty of Biology, Institute of Microbiology, University of Warsaw, 02-096 Warsaw, PolandLaboratory of Biological Chemistry of Metal Ions, Institute of Biochemistry and Biophysics, Polish Academy of Sciences, 02-106 Warsaw, PolandFaculty of Chemistry, University of Gdańsk, 80-308 Gdansk, PolandDepartment of Animal Physiology, Faculty of Biology, Institute of Functional Biology and Ecology, University of Warsaw, 02-096 Warsaw, PolandMass Spectrometry Laboratory, Institute of Biochemistry and Biophysics, Polish Academy of Sciences, 02-106 Warsaw, PolandDepartment of Bacterial Genetics, Faculty of Biology, Institute of Microbiology, University of Warsaw, 02-096 Warsaw, PolandThe bacterial proteins of the Dsb family catalyze the formation of disulfide bridges between cysteine residues that stabilize protein structures and ensure their proper functioning. Here, we report the detailed analysis of the Dsb pathway of <i>Campylobacter jejuni</i>. The oxidizing Dsb system of this pathogen is unique because it consists of two monomeric DsbAs (DsbA1 and DsbA2) and one dimeric bifunctional protein (C8J_1298). Previously, we showed that DsbA1 and C8J_1298 are redundant. Here, we unraveled the interaction between the two monomeric DsbAs by in vitro and in vivo experiments and by solving their structures and found that both monomeric DsbAs are dispensable proteins. Their structures confirmed that they are homologs of EcDsbL. The slight differences seen in the surface charge of the proteins do not affect the interaction with their redox partner. Comparative proteomics showed that several respiratory proteins, as well as periplasmic transport proteins, are targets of the Dsb system. Some of these, both donors and electron acceptors, are essential elements of the <i>C. jejuni</i> respiratory process under oxygen-limiting conditions in the host intestine. The data presented provide detailed information on the function of the <i>C. jejuni</i> Dsb system, identifying it as a potential target for novel antibacterial molecules.https://www.mdpi.com/1422-0067/22/24/13451disulfide bondthiol oxidoreductaseDsb proteins<i>Campylobacter jejuni</i>crystal structuresubstrates |
| spellingShingle | Anna M. Banaś Katarzyna M. Bocian-Ostrzycka Stanisław Dunin-Horkawicz Jan Ludwiczak Piotr Wilk Marta Orlikowska Agnieszka Wyszyńska Maria Dąbrowska Maciej Plichta Marta Spodzieja Marta A. Polańska Agata Malinowska Elżbieta Katarzyna Jagusztyn-Krynicka Interplay between DsbA1, DsbA2 and C8J_1298 Periplasmic Oxidoreductases of <i>Campylobacter jejuni</i> and Their Impact on Bacterial Physiology and Pathogenesis International Journal of Molecular Sciences disulfide bond thiol oxidoreductase Dsb proteins <i>Campylobacter jejuni</i> crystal structure substrates |
| title | Interplay between DsbA1, DsbA2 and C8J_1298 Periplasmic Oxidoreductases of <i>Campylobacter jejuni</i> and Their Impact on Bacterial Physiology and Pathogenesis |
| title_full | Interplay between DsbA1, DsbA2 and C8J_1298 Periplasmic Oxidoreductases of <i>Campylobacter jejuni</i> and Their Impact on Bacterial Physiology and Pathogenesis |
| title_fullStr | Interplay between DsbA1, DsbA2 and C8J_1298 Periplasmic Oxidoreductases of <i>Campylobacter jejuni</i> and Their Impact on Bacterial Physiology and Pathogenesis |
| title_full_unstemmed | Interplay between DsbA1, DsbA2 and C8J_1298 Periplasmic Oxidoreductases of <i>Campylobacter jejuni</i> and Their Impact on Bacterial Physiology and Pathogenesis |
| title_short | Interplay between DsbA1, DsbA2 and C8J_1298 Periplasmic Oxidoreductases of <i>Campylobacter jejuni</i> and Their Impact on Bacterial Physiology and Pathogenesis |
| title_sort | interplay between dsba1 dsba2 and c8j 1298 periplasmic oxidoreductases of i campylobacter jejuni i and their impact on bacterial physiology and pathogenesis |
| topic | disulfide bond thiol oxidoreductase Dsb proteins <i>Campylobacter jejuni</i> crystal structure substrates |
| url | https://www.mdpi.com/1422-0067/22/24/13451 |
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