Each Cellular Compartment Has a Characteristic Protein Reactive Cysteine Ratio Determining Its Sensitivity to Oxidation
Signaling and detoxification of Reactive Oxygen Species (ROS) are important patho-physiologcal processes. Despite this, we lack comprehensive information on individual cells and cellular structures and functions affected by ROS, which is essential to build quantitative models of the effects of ROS....
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| Format: | Article |
| Language: | English |
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MDPI AG
2023-06-01
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| Series: | Antioxidants |
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| Online Access: | https://www.mdpi.com/2076-3921/12/6/1274 |
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| author | Ricardo Pires das Neves Mónica Chagoyen Antonio Martinez-Lorente Carlos Iñiguez Ana Calatrava Juana Calabuig Francisco J. Iborra |
| author_facet | Ricardo Pires das Neves Mónica Chagoyen Antonio Martinez-Lorente Carlos Iñiguez Ana Calatrava Juana Calabuig Francisco J. Iborra |
| author_sort | Ricardo Pires das Neves |
| collection | DOAJ |
| description | Signaling and detoxification of Reactive Oxygen Species (ROS) are important patho-physiologcal processes. Despite this, we lack comprehensive information on individual cells and cellular structures and functions affected by ROS, which is essential to build quantitative models of the effects of ROS. The thiol groups from cysteines (Cys) in proteins play a major role in redox defense, signaling, and protein function. In this study, we show that the proteins in each subcellular compartment contain a characteristic Cys amount. Using a fluorescent assay for -SH in thiolate form and amino groups in proteins, we show that the thiolate content correlates with ROS sensitivity and signaling properties of each compartment. The highest absolute thiolate concentration was found in the nucleolus, followed by the nucleoplasm and cytoplasm whereas protein thiolate groups per protein showed an inverse pattern. In the nucleoplasm, protein reactive thiols concentrated in SC35 speckles, SMN, and the IBODY that accumulated oxidized RNA. Our findings have important functional consequences, and explain differential sensitivity to ROS. |
| first_indexed | 2024-03-11T02:50:00Z |
| format | Article |
| id | doaj.art-b02ebaa97a214756a59820e2df82b197 |
| institution | Directory Open Access Journal |
| issn | 2076-3921 |
| language | English |
| last_indexed | 2024-03-11T02:50:00Z |
| publishDate | 2023-06-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Antioxidants |
| spelling | doaj.art-b02ebaa97a214756a59820e2df82b1972023-11-18T09:03:54ZengMDPI AGAntioxidants2076-39212023-06-01126127410.3390/antiox12061274Each Cellular Compartment Has a Characteristic Protein Reactive Cysteine Ratio Determining Its Sensitivity to OxidationRicardo Pires das Neves0Mónica Chagoyen1Antonio Martinez-Lorente2Carlos Iñiguez3Ana Calatrava4Juana Calabuig5Francisco J. Iborra6Center for Neuroscience and Cell Biology, CIBB—Centre for Innovative Biomedicine and Biotechnology, University of Coimbra, 3004-517 Coimbra, PortugalCentro Nacional de Biotecnología, CSIC, Darwin 3, 28049 Madrid, SpainUnidad de Investigación, Innovación y Docencia Médica, Hospital Universitario Vinalopó, 03293 Elx, SpainDepartment of Biotecnology, University of Alicante, 03690 Alicante, SpainDepartment of Pathology, Fundación Instituto Valenciano de Oncología, 46009 Valencia, SpainIC Biomed, 03638 Salinas, SpainInstituto de Biomedicina de Valencia, CSIC, Jaime Roig 11, 46010 Valencia, SpainSignaling and detoxification of Reactive Oxygen Species (ROS) are important patho-physiologcal processes. Despite this, we lack comprehensive information on individual cells and cellular structures and functions affected by ROS, which is essential to build quantitative models of the effects of ROS. The thiol groups from cysteines (Cys) in proteins play a major role in redox defense, signaling, and protein function. In this study, we show that the proteins in each subcellular compartment contain a characteristic Cys amount. Using a fluorescent assay for -SH in thiolate form and amino groups in proteins, we show that the thiolate content correlates with ROS sensitivity and signaling properties of each compartment. The highest absolute thiolate concentration was found in the nucleolus, followed by the nucleoplasm and cytoplasm whereas protein thiolate groups per protein showed an inverse pattern. In the nucleoplasm, protein reactive thiols concentrated in SC35 speckles, SMN, and the IBODY that accumulated oxidized RNA. Our findings have important functional consequences, and explain differential sensitivity to ROS.https://www.mdpi.com/2076-3921/12/6/1274oxidative stressnuclear specklesSMNRNA polymerasetranscription8-hydroxy guanosine |
| spellingShingle | Ricardo Pires das Neves Mónica Chagoyen Antonio Martinez-Lorente Carlos Iñiguez Ana Calatrava Juana Calabuig Francisco J. Iborra Each Cellular Compartment Has a Characteristic Protein Reactive Cysteine Ratio Determining Its Sensitivity to Oxidation Antioxidants oxidative stress nuclear speckles SMN RNA polymerase transcription 8-hydroxy guanosine |
| title | Each Cellular Compartment Has a Characteristic Protein Reactive Cysteine Ratio Determining Its Sensitivity to Oxidation |
| title_full | Each Cellular Compartment Has a Characteristic Protein Reactive Cysteine Ratio Determining Its Sensitivity to Oxidation |
| title_fullStr | Each Cellular Compartment Has a Characteristic Protein Reactive Cysteine Ratio Determining Its Sensitivity to Oxidation |
| title_full_unstemmed | Each Cellular Compartment Has a Characteristic Protein Reactive Cysteine Ratio Determining Its Sensitivity to Oxidation |
| title_short | Each Cellular Compartment Has a Characteristic Protein Reactive Cysteine Ratio Determining Its Sensitivity to Oxidation |
| title_sort | each cellular compartment has a characteristic protein reactive cysteine ratio determining its sensitivity to oxidation |
| topic | oxidative stress nuclear speckles SMN RNA polymerase transcription 8-hydroxy guanosine |
| url | https://www.mdpi.com/2076-3921/12/6/1274 |
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