Correction to: Thiol-Redox Proteomics to Study Reversible Protein Thiol Oxidations in Bacteria.

This protocol was originally published © Springer Science+Business Media, LLC, part of Springer Nature 2018, but has now been made available © The Author(s) under a CC BY 4.0 license.

Thiol-Redox Proteomics to Study Reversible Protein Thiol Oxidations in Bacteria.

Thiol-redox proteomics methods are rapidly developing tools in redox biology. These are applied to identify and quantify proteins with reversible thiol oxidations that are formed under normal growth and oxidative stress conditions inside cells. The proteins with reversible thiol oxidations are usually prepared by alkylation of reduced thiols, subsequent reduction of disulfide bonds followed by a second differential alkylation of newly released thiols.

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.

50 years to diagnosis: Autosomal dominant tubular aggregate myopathy caused by a novel STIM1 mutation.

Tubular aggregates in human muscle biopsies have been reported to occur in a variety of acquired and hereditary neuromuscular conditions since 1964. Recently mutations in the gene encoding the main calcium sensor in the sarcoplasmic reticulum, stromal interaction molecule 1 (STIM1), have been identified as a cause of autosomal dominant tubular aggregate myopathy. We studied a German family with tubular aggregate myopathy and defined cellular consequences of altered STIM1 function.

Redox regulation by reversible protein S-thiolation in bacteria.

Low molecular weight (LMW) thiols function as thiol-redox buffers to maintain the reduced state of the cytoplasm. The best studied LMW thiol is the tripeptide glutathione (GSH) present in all eukaryotes and Gram-negative bacteria. Firmicutes bacteria, including Bacillus and Staphylococcus species utilize the redox buffer bacillithiol (BSH) while Actinomycetes produce the related redox buffer mycothiol (MSH).