Redox proteomics reveal a role for peroxiredoxinylation in stress protection
Summary: The redox state of proteins is essential for their function and guarantees cell fitness. Peroxiredoxins protect cells against oxidative stress, maintain redox homeostasis, act as chaperones, and transmit hydrogen peroxide signals to redox regulators. Despite the profound structural and func...
Saved in:
| Main Authors: | , , , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Elsevier
2025-02-01
|
| Series: | Cell Reports |
| Subjects: | |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S2211124724015754 |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
| _version_ | 1832590989306363904 |
|---|---|
| author | Gerhard Seisenbacher Zrinka Raguz Nakic Eva Borràs Eduard Sabidó Uwe Sauer Eulalia de Nadal Francesc Posas |
| author_facet | Gerhard Seisenbacher Zrinka Raguz Nakic Eva Borràs Eduard Sabidó Uwe Sauer Eulalia de Nadal Francesc Posas |
| author_sort | Gerhard Seisenbacher |
| collection | DOAJ |
| description | Summary: The redox state of proteins is essential for their function and guarantees cell fitness. Peroxiredoxins protect cells against oxidative stress, maintain redox homeostasis, act as chaperones, and transmit hydrogen peroxide signals to redox regulators. Despite the profound structural and functional knowledge of peroxiredoxins action, information on how the different functions are concerted is still scarce. Using global proteomic analyses, we show here that the yeast peroxiredoxin Tsa1 interacts with many proteins of essential biological processes, including protein turnover and carbohydrate metabolism. Several of these interactions are of a covalent nature, and we show that failure of peroxiredoxinylation of Gnd1 affects its phosphogluconate dehydrogenase activity and impairs recovery upon stress. Thioredoxins directly remove TSA1-formed mixed disulfide intermediates, thus expanding the role of the thioredoxin-peroxiredoxin redox cycle pair to buffer the redox state of proteins. |
| format | Article |
| id | doaj-art-c9a7e0cdc2fc4d71b051bf001ca26309 |
| institution | Kabale University |
| issn | 2211-1247 |
| language | English |
| publishDate | 2025-02-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Cell Reports |
| spelling | doaj-art-c9a7e0cdc2fc4d71b051bf001ca263092025-01-23T05:26:37ZengElsevierCell Reports2211-12472025-02-01442115224Redox proteomics reveal a role for peroxiredoxinylation in stress protectionGerhard Seisenbacher0Zrinka Raguz Nakic1Eva Borràs2Eduard Sabidó3Uwe Sauer4Eulalia de Nadal5Francesc Posas6Department of Medicine and Life Sciences, Universitat Pompeu Fabra, 08003 Barcelona, Spain; Institute for Research in Biomedicine (IRB Barcelona), Barcelona Institute of Science and Technology, 08028 Barcelona, SpainInstitute of Molecular Systems Biology, ETH Zürich, 8093 Zurich, Switzerland; ZHAW School of Life Sciences and Facility Management, Biosystems Technology, 8820 Wädenswil, SwitzerlandDepartment of Medicine and Life Sciences, Universitat Pompeu Fabra, 08003 Barcelona, Spain; Centre of Genomic Regulation, Barcelona Institute of Science and Technology, 08003 Barcelona, SpainDepartment of Medicine and Life Sciences, Universitat Pompeu Fabra, 08003 Barcelona, Spain; Centre of Genomic Regulation, Barcelona Institute of Science and Technology, 08003 Barcelona, SpainInstitute of Molecular Systems Biology, ETH Zürich, 8093 Zurich, SwitzerlandDepartment of Medicine and Life Sciences, Universitat Pompeu Fabra, 08003 Barcelona, Spain; Institute for Research in Biomedicine (IRB Barcelona), Barcelona Institute of Science and Technology, 08028 Barcelona, Spain; Corresponding authorDepartment of Medicine and Life Sciences, Universitat Pompeu Fabra, 08003 Barcelona, Spain; Institute for Research in Biomedicine (IRB Barcelona), Barcelona Institute of Science and Technology, 08028 Barcelona, Spain; Corresponding authorSummary: The redox state of proteins is essential for their function and guarantees cell fitness. Peroxiredoxins protect cells against oxidative stress, maintain redox homeostasis, act as chaperones, and transmit hydrogen peroxide signals to redox regulators. Despite the profound structural and functional knowledge of peroxiredoxins action, information on how the different functions are concerted is still scarce. Using global proteomic analyses, we show here that the yeast peroxiredoxin Tsa1 interacts with many proteins of essential biological processes, including protein turnover and carbohydrate metabolism. Several of these interactions are of a covalent nature, and we show that failure of peroxiredoxinylation of Gnd1 affects its phosphogluconate dehydrogenase activity and impairs recovery upon stress. Thioredoxins directly remove TSA1-formed mixed disulfide intermediates, thus expanding the role of the thioredoxin-peroxiredoxin redox cycle pair to buffer the redox state of proteins.http://www.sciencedirect.com/science/article/pii/S2211124724015754CP: Molecular biology |
| spellingShingle | Gerhard Seisenbacher Zrinka Raguz Nakic Eva Borràs Eduard Sabidó Uwe Sauer Eulalia de Nadal Francesc Posas Redox proteomics reveal a role for peroxiredoxinylation in stress protection Cell Reports CP: Molecular biology |
| title | Redox proteomics reveal a role for peroxiredoxinylation in stress protection |
| title_full | Redox proteomics reveal a role for peroxiredoxinylation in stress protection |
| title_fullStr | Redox proteomics reveal a role for peroxiredoxinylation in stress protection |
| title_full_unstemmed | Redox proteomics reveal a role for peroxiredoxinylation in stress protection |
| title_short | Redox proteomics reveal a role for peroxiredoxinylation in stress protection |
| title_sort | redox proteomics reveal a role for peroxiredoxinylation in stress protection |
| topic | CP: Molecular biology |
| url | http://www.sciencedirect.com/science/article/pii/S2211124724015754 |
| work_keys_str_mv | AT gerhardseisenbacher redoxproteomicsrevealaroleforperoxiredoxinylationinstressprotection AT zrinkaraguznakic redoxproteomicsrevealaroleforperoxiredoxinylationinstressprotection AT evaborras redoxproteomicsrevealaroleforperoxiredoxinylationinstressprotection AT eduardsabido redoxproteomicsrevealaroleforperoxiredoxinylationinstressprotection AT uwesauer redoxproteomicsrevealaroleforperoxiredoxinylationinstressprotection AT eulaliadenadal redoxproteomicsrevealaroleforperoxiredoxinylationinstressprotection AT francescposas redoxproteomicsrevealaroleforperoxiredoxinylationinstressprotection |