The Multifaceted Bacterial Cysteine Desulfurases: From Metabolism to Pathogenesis
Living cells have developed a relay system to efficiently transfer sulfur (S) from cysteine to various thio-cofactors (iron-sulfur (Fe-S) clusters, thiamine, molybdopterin, lipoic acid, and biotin) and thiolated tRNA. The presence of such a transit route involves multiple protein components that all...
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| Format: | Article |
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MDPI AG
2021-06-01
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| Series: | Antioxidants |
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| Online Access: | https://www.mdpi.com/2076-3921/10/7/997 |
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| author | Mayashree Das Arshiya Dewan Somnath Shee Amit Singh |
| author_facet | Mayashree Das Arshiya Dewan Somnath Shee Amit Singh |
| author_sort | Mayashree Das |
| collection | DOAJ |
| description | Living cells have developed a relay system to efficiently transfer sulfur (S) from cysteine to various thio-cofactors (iron-sulfur (Fe-S) clusters, thiamine, molybdopterin, lipoic acid, and biotin) and thiolated tRNA. The presence of such a transit route involves multiple protein components that allow the flux of S to be precisely regulated as a function of environmental cues to avoid the unnecessary accumulation of toxic concentrations of soluble sulfide (S<sup>2−</sup>). The first enzyme in this relay system is cysteine desulfurase (CSD). CSD catalyzes the release of sulfane S from L-cysteine by converting it to L-alanine by forming an enzyme-linked persulfide intermediate on its conserved cysteine residue. The persulfide S is then transferred to diverse acceptor proteins for its incorporation into the thio-cofactors. The thio-cofactor binding-proteins participate in essential and diverse cellular processes, including DNA repair, respiration, intermediary metabolism, gene regulation, and redox sensing. Additionally, CSD modulates pathogenesis, antibiotic susceptibility, metabolism, and survival of several pathogenic microbes within their hosts. In this review, we aim to comprehensively illustrate the impact of CSD on bacterial core metabolic processes and its requirement to combat redox stresses and antibiotics. Targeting CSD in human pathogens can be a potential therapy for better treatment outcomes. |
| first_indexed | 2024-03-10T10:08:49Z |
| format | Article |
| id | doaj.art-bf690d7907714befb49874b5521091ab |
| institution | Directory Open Access Journal |
| issn | 2076-3921 |
| language | English |
| last_indexed | 2024-03-10T10:08:49Z |
| publishDate | 2021-06-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Antioxidants |
| spelling | doaj.art-bf690d7907714befb49874b5521091ab2023-11-22T01:19:41ZengMDPI AGAntioxidants2076-39212021-06-0110799710.3390/antiox10070997The Multifaceted Bacterial Cysteine Desulfurases: From Metabolism to PathogenesisMayashree Das0Arshiya Dewan1Somnath Shee2Amit Singh3Centre for Infectious Disease Research, Department of Microbiology and Cell Biology, Indian Institute of Science, Bangalore 560012, IndiaCentre for Infectious Disease Research, Department of Microbiology and Cell Biology, Indian Institute of Science, Bangalore 560012, IndiaCentre for Infectious Disease Research, Department of Microbiology and Cell Biology, Indian Institute of Science, Bangalore 560012, IndiaCentre for Infectious Disease Research, Department of Microbiology and Cell Biology, Indian Institute of Science, Bangalore 560012, IndiaLiving cells have developed a relay system to efficiently transfer sulfur (S) from cysteine to various thio-cofactors (iron-sulfur (Fe-S) clusters, thiamine, molybdopterin, lipoic acid, and biotin) and thiolated tRNA. The presence of such a transit route involves multiple protein components that allow the flux of S to be precisely regulated as a function of environmental cues to avoid the unnecessary accumulation of toxic concentrations of soluble sulfide (S<sup>2−</sup>). The first enzyme in this relay system is cysteine desulfurase (CSD). CSD catalyzes the release of sulfane S from L-cysteine by converting it to L-alanine by forming an enzyme-linked persulfide intermediate on its conserved cysteine residue. The persulfide S is then transferred to diverse acceptor proteins for its incorporation into the thio-cofactors. The thio-cofactor binding-proteins participate in essential and diverse cellular processes, including DNA repair, respiration, intermediary metabolism, gene regulation, and redox sensing. Additionally, CSD modulates pathogenesis, antibiotic susceptibility, metabolism, and survival of several pathogenic microbes within their hosts. In this review, we aim to comprehensively illustrate the impact of CSD on bacterial core metabolic processes and its requirement to combat redox stresses and antibiotics. Targeting CSD in human pathogens can be a potential therapy for better treatment outcomes.https://www.mdpi.com/2076-3921/10/7/997cysteine desulfurase (CSD)Fe-S clusterredoxthio-cofactorsROS |
| spellingShingle | Mayashree Das Arshiya Dewan Somnath Shee Amit Singh The Multifaceted Bacterial Cysteine Desulfurases: From Metabolism to Pathogenesis Antioxidants cysteine desulfurase (CSD) Fe-S cluster redox thio-cofactors ROS |
| title | The Multifaceted Bacterial Cysteine Desulfurases: From Metabolism to Pathogenesis |
| title_full | The Multifaceted Bacterial Cysteine Desulfurases: From Metabolism to Pathogenesis |
| title_fullStr | The Multifaceted Bacterial Cysteine Desulfurases: From Metabolism to Pathogenesis |
| title_full_unstemmed | The Multifaceted Bacterial Cysteine Desulfurases: From Metabolism to Pathogenesis |
| title_short | The Multifaceted Bacterial Cysteine Desulfurases: From Metabolism to Pathogenesis |
| title_sort | multifaceted bacterial cysteine desulfurases from metabolism to pathogenesis |
| topic | cysteine desulfurase (CSD) Fe-S cluster redox thio-cofactors ROS |
| url | https://www.mdpi.com/2076-3921/10/7/997 |
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