dc.contributor.author
Hillion, Melanie
dc.contributor.author
Bernhardt, Jörg
dc.contributor.author
Busche, Tobias
dc.contributor.author
Rossius, Martina
dc.contributor.author
Maass, Sandra
dc.contributor.author
Becher, Dörte
dc.contributor.author
Rawat, Mamta
dc.contributor.author
Wirtz, Markus
dc.contributor.author
Hell, Rüdiger
dc.contributor.author
Rückert, Christian
dc.contributor.author
Kalinowski, Jörn
dc.contributor.author
Antelmann, Haike
dc.date.accessioned
2018-06-08T10:42:35Z
dc.date.available
2017-07-03T08:06:37.409Z
dc.identifier.uri
https://refubium.fu-berlin.de/handle/fub188/20930
dc.identifier.uri
http://dx.doi.org/10.17169/refubium-24229
dc.description.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.
en
dc.rights.uri
http://creativecommons.org/licenses/by/4.0/
dc.subject
Bacterial systems biology
dc.subject
Protein–protein interaction networks
dc.subject.ddc
500 Naturwissenschaften und Mathematik::570 Biowissenschaften; Biologie
dc.title
Monitoring global protein thiol-oxidation and protein S-mycothiolation in
Mycobacterium smegmatis under hypochlorite stress
dc.type
Wissenschaftlicher Artikel
dcterms.bibliographicCitation
Scientific Reports. - 7 (2017), Artikel Nr. 1195
dcterms.bibliographicCitation.doi
10.1038/s41598-017-01179-4
dcterms.bibliographicCitation.url
http://www.nature.com/articles/s41598-017-01179-4
refubium.affiliation
Biologie, Chemie, Pharmazie
de
refubium.mycore.fudocsId
FUDOCS_document_000000027089
refubium.note.author
Der Artikel wurde in einer reinen Open-Access-Zeitschrift publiziert.
refubium.resourceType.isindependentpub
no
refubium.mycore.derivateId
FUDOCS_derivate_000000008253
dcterms.accessRights.openaire
open access