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Monitoring global protein thiol-oxidation and protein S- mycothiolation in Mycobacterium smegmatis under hypochlorite stress
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| Veröffentlicht in: | Scientific reports 7(2017) article number 1195, 20 Seiten |
|---|---|
| Personen und Körperschaften: | , , |
| Titel: | Monitoring global protein thiol-oxidation and protein S- mycothiolation in Mycobacterium smegmatis under hypochlorite stress/ Melanie Hillion, Jörg Bernhardt, Tobias Busche, Martina Rossius, Sandra Maaß, Dörte Becher, Mamta Rawat, Markus Wirtz, Rüdiger Hell, Christian Rückert, Jörn Kalinowski & Haike Antelmann |
| Format: | E-Book-Kapitel |
| Sprache: | Englisch |
| veröffentlicht: |
2017
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| Gesamtaufnahme: |
: Scientific reports, 7(2017) article number 1195, 20 Seiten
, volume:7 |
| Quelle: | Verbunddaten SWB Lizenzfreie Online-Ressourcen |
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| 245 | 1 | 0 | |a Monitoring global protein thiol-oxidation and protein S- mycothiolation in Mycobacterium smegmatis under hypochlorite stress |c Melanie Hillion, Jörg Bernhardt, Tobias Busche, Martina Rossius, Sandra Maaß, Dörte Becher, Mamta Rawat, Markus Wirtz, Rüdiger Hell, Christian Rückert, Jörn Kalinowski & Haike Antelmann |
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| 520 | |a Mycothiol (MSH) is the major low molecular weight (LMW) thiol in Actinomycetes. Here, we used shotgun proteomics, OxICAT and RNA-seq transcriptomics to analyse protein S-mycothiolation, reversible thiol-oxidations and their impact on gene expression in Mycobacterium smegmatis under hypochlorite stress. In total, 58 S-mycothiolated proteins were identified under NaOCl stress that are involved in energy metabolism, fatty acid and mycolic acid biosynthesis, protein translation, redox regulation and detoxification. Protein S-mycothiolation was accompanied by MSH depletion in the thiol-metabolome. Quantification of the redox state of 1098 Cys residues using OxICAT revealed that 381 Cys residues (33.6%) showed >10% increased oxidations under NaOCl stress, which overlapped with 40 S-mycothiolated Cys-peptides. The absence of MSH resulted in a higher basal oxidation level of 338 Cys residues (41.1%). The RseA and RshA anti-sigma factors and the Zur and NrdR repressors were identified as NaOCl-sensitive proteins and their oxidation resulted in an up-regulation of the SigH, SigE, Zur and NrdR regulons in the RNA-seq transcriptome. In conclusion, we show here that NaOCl stress causes widespread thiol-oxidation including protein S-mycothiolation resulting in induction of antioxidant defense mechanisms in M. smegmatis. Our results further reveal that MSH is important to maintain the reduced state of protein thiols. | ||
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| contents | Mycothiol (MSH) is the major low molecular weight (LMW) thiol in Actinomycetes. Here, we used shotgun proteomics, OxICAT and RNA-seq transcriptomics to analyse protein S-mycothiolation, reversible thiol-oxidations and their impact on gene expression in Mycobacterium smegmatis under hypochlorite stress. In total, 58 S-mycothiolated proteins were identified under NaOCl stress that are involved in energy metabolism, fatty acid and mycolic acid biosynthesis, protein translation, redox regulation and detoxification. Protein S-mycothiolation was accompanied by MSH depletion in the thiol-metabolome. Quantification of the redox state of 1098 Cys residues using OxICAT revealed that 381 Cys residues (33.6%) showed >10% increased oxidations under NaOCl stress, which overlapped with 40 S-mycothiolated Cys-peptides. The absence of MSH resulted in a higher basal oxidation level of 338 Cys residues (41.1%). The RseA and RshA anti-sigma factors and the Zur and NrdR repressors were identified as NaOCl-sensitive proteins and their oxidation resulted in an up-regulation of the SigH, SigE, Zur and NrdR regulons in the RNA-seq transcriptome. In conclusion, we show here that NaOCl stress causes widespread thiol-oxidation including protein S-mycothiolation resulting in induction of antioxidant defense mechanisms in M. smegmatis. Our results further reveal that MSH is important to maintain the reduced state of protein thiols. |
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| footnote | Published online: 26 April 2017, Gesehen am 22.06.2018 |
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| spelling | Hillion, Melanie VerfasserIn (DE-588)1161612572 (DE-627)1024897648 (DE-576)506759628 aut, Monitoring global protein thiol-oxidation and protein S- mycothiolation in Mycobacterium smegmatis under hypochlorite stress Melanie Hillion, Jörg Bernhardt, Tobias Busche, Martina Rossius, Sandra Maaß, Dörte Becher, Mamta Rawat, Markus Wirtz, Rüdiger Hell, Christian Rückert, Jörn Kalinowski & Haike Antelmann, 2017, 20, Text txt rdacontent, Computermedien c rdamedia, Online-Ressource cr rdacarrier, Published online: 26 April 2017, Gesehen am 22.06.2018, Mycothiol (MSH) is the major low molecular weight (LMW) thiol in Actinomycetes. Here, we used shotgun proteomics, OxICAT and RNA-seq transcriptomics to analyse protein S-mycothiolation, reversible thiol-oxidations and their impact on gene expression in Mycobacterium smegmatis under hypochlorite stress. In total, 58 S-mycothiolated proteins were identified under NaOCl stress that are involved in energy metabolism, fatty acid and mycolic acid biosynthesis, protein translation, redox regulation and detoxification. Protein S-mycothiolation was accompanied by MSH depletion in the thiol-metabolome. Quantification of the redox state of 1098 Cys residues using OxICAT revealed that 381 Cys residues (33.6%) showed >10% increased oxidations under NaOCl stress, which overlapped with 40 S-mycothiolated Cys-peptides. The absence of MSH resulted in a higher basal oxidation level of 338 Cys residues (41.1%). The RseA and RshA anti-sigma factors and the Zur and NrdR repressors were identified as NaOCl-sensitive proteins and their oxidation resulted in an up-regulation of the SigH, SigE, Zur and NrdR regulons in the RNA-seq transcriptome. In conclusion, we show here that NaOCl stress causes widespread thiol-oxidation including protein S-mycothiolation resulting in induction of antioxidant defense mechanisms in M. smegmatis. Our results further reveal that MSH is important to maintain the reduced state of protein thiols., Wirtz, Markus VerfasserIn (DE-588)1023118378 (DE-627)717709353 (DE-576)36641979X aut, Hell, Rüdiger VerfasserIn (DE-588)1022964933 (DE-627)717340341 (DE-576)166399647 aut, Enthalten in Scientific reports [London] : Macmillan Publishers Limited, part of Springer Nature, 2011 7(2017) article number 1195, 20 Seiten Online-Ressource (DE-627)663366712 (DE-600)2615211-3 (DE-576)346641179 2045-2322 nnns, volume:7 year:2017 pages:1195 extent:20, http://dx.doi.org/10.1038/s41598-017-01179-4 Verlag kostenfrei Volltext, https://www.nature.com/articles/s41598-017-01179-4 Verlag kostenfrei Volltext, http://dx.doi.org/10.1038/s41598-017-01179-4 LFER, LFER 2018-07-10T00:00:00Z |
| spellingShingle | Hillion, Melanie, Wirtz, Markus, Hell, Rüdiger, Monitoring global protein thiol-oxidation and protein S- mycothiolation in Mycobacterium smegmatis under hypochlorite stress, Mycothiol (MSH) is the major low molecular weight (LMW) thiol in Actinomycetes. Here, we used shotgun proteomics, OxICAT and RNA-seq transcriptomics to analyse protein S-mycothiolation, reversible thiol-oxidations and their impact on gene expression in Mycobacterium smegmatis under hypochlorite stress. In total, 58 S-mycothiolated proteins were identified under NaOCl stress that are involved in energy metabolism, fatty acid and mycolic acid biosynthesis, protein translation, redox regulation and detoxification. Protein S-mycothiolation was accompanied by MSH depletion in the thiol-metabolome. Quantification of the redox state of 1098 Cys residues using OxICAT revealed that 381 Cys residues (33.6%) showed >10% increased oxidations under NaOCl stress, which overlapped with 40 S-mycothiolated Cys-peptides. The absence of MSH resulted in a higher basal oxidation level of 338 Cys residues (41.1%). The RseA and RshA anti-sigma factors and the Zur and NrdR repressors were identified as NaOCl-sensitive proteins and their oxidation resulted in an up-regulation of the SigH, SigE, Zur and NrdR regulons in the RNA-seq transcriptome. In conclusion, we show here that NaOCl stress causes widespread thiol-oxidation including protein S-mycothiolation resulting in induction of antioxidant defense mechanisms in M. smegmatis. Our results further reveal that MSH is important to maintain the reduced state of protein thiols. |
| swb_id_str | 506759776 |
| title | Monitoring global protein thiol-oxidation and protein S- mycothiolation in Mycobacterium smegmatis under hypochlorite stress |
| title_auth | Monitoring global protein thiol-oxidation and protein S- mycothiolation in Mycobacterium smegmatis under hypochlorite stress |
| title_full | Monitoring global protein thiol-oxidation and protein S- mycothiolation in Mycobacterium smegmatis under hypochlorite stress Melanie Hillion, Jörg Bernhardt, Tobias Busche, Martina Rossius, Sandra Maaß, Dörte Becher, Mamta Rawat, Markus Wirtz, Rüdiger Hell, Christian Rückert, Jörn Kalinowski & Haike Antelmann |
| title_fullStr | Monitoring global protein thiol-oxidation and protein S- mycothiolation in Mycobacterium smegmatis under hypochlorite stress Melanie Hillion, Jörg Bernhardt, Tobias Busche, Martina Rossius, Sandra Maaß, Dörte Becher, Mamta Rawat, Markus Wirtz, Rüdiger Hell, Christian Rückert, Jörn Kalinowski & Haike Antelmann |
| title_full_unstemmed | Monitoring global protein thiol-oxidation and protein S- mycothiolation in Mycobacterium smegmatis under hypochlorite stress Melanie Hillion, Jörg Bernhardt, Tobias Busche, Martina Rossius, Sandra Maaß, Dörte Becher, Mamta Rawat, Markus Wirtz, Rüdiger Hell, Christian Rückert, Jörn Kalinowski & Haike Antelmann |
| title_in_hierarchy | Monitoring global protein thiol-oxidation and protein S- mycothiolation in Mycobacterium smegmatis under hypochlorite stress / Melanie Hillion, Jörg Bernhardt, Tobias Busche, Martina Rossius, Sandra Maaß, Dörte Becher, Mamta Rawat, Markus Wirtz, Rüdiger Hell, Christian Rückert, Jörn Kalinowski & Haike Antelmann, |
| title_short | Monitoring global protein thiol-oxidation and protein S- mycothiolation in Mycobacterium smegmatis under hypochlorite stress |
| title_sort | monitoring global protein thiol oxidation and protein s mycothiolation in mycobacterium smegmatis under hypochlorite stress |
| url | http://dx.doi.org/10.1038/s41598-017-01179-4, https://www.nature.com/articles/s41598-017-01179-4 |