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Verfasst von:Hillion, Melanie [VerfasserIn]   i
 Wirtz, Markus [VerfasserIn]   i
 Hell, Rüdiger [VerfasserIn]   i
Titel:Monitoring global protein thiol-oxidation and protein S- mycothiolation in Mycobacterium smegmatis under hypochlorite stress
Verf.angabe:Melanie Hillion, Jörg Bernhardt, Tobias Busche, Martina Rossius, Sandra Maaß, Dörte Becher, Mamta Rawat, Markus Wirtz, Rüdiger Hell, Christian Rückert, Jörn Kalinowski & Haike Antelmann
Jahr:2017
Umfang:20 S.
Fussnoten:Published online: 26 April 2017 ; Gesehen am 22.06.2018
Titel Quelle:Enthalten in: Scientific reports
Ort Quelle:[London] : Macmillan Publishers Limited, part of Springer Nature, 2011
Jahr Quelle:2017
Band/Heft Quelle:7(2017) article number 1195, 20 Seiten
ISSN Quelle:2045-2322
Abstract: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.
DOI:doi:10.1038/s41598-017-01179-4
URL:Bitte beachten Sie: Dies ist ein Bibliographieeintrag. Ein Volltextzugriff für Mitglieder der Universität besteht hier nur, falls für die entsprechende Zeitschrift/den entsprechenden Sammelband ein Abonnement besteht oder es sich um einen OpenAccess-Titel handelt.

Kostenfrei: Volltext ; Verlag: http://dx.doi.org/10.1038/s41598-017-01179-4
 Kostenfrei: Volltext: https://www.nature.com/articles/s41598-017-01179-4
 DOI: https://doi.org/10.1038/s41598-017-01179-4
Datenträger:Online-Ressource
Sprache:eng
K10plus-PPN:1576759776
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