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Redox regulation by reversible protein S-thiolation in Gram-positive bacteria
Low molecular weight (LMW) thiols play an important role as thiol-cofactors for many enzymes and are crucial to maintain the reduced state of the cytoplasm. Most Gram-negative bacteria utilize glutathione (GSH) as major LMW thiol. However, in Gram-positive Actinomycetes and Firmicutes alternative LM...
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6178380/ https://www.ncbi.nlm.nih.gov/pubmed/30308476 http://dx.doi.org/10.1016/j.redox.2018.08.017 |
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author | Imber, Marcel Pietrzyk-Brzezinska, Agnieszka J. Antelmann, Haike |
author_facet | Imber, Marcel Pietrzyk-Brzezinska, Agnieszka J. Antelmann, Haike |
author_sort | Imber, Marcel |
collection | PubMed |
description | Low molecular weight (LMW) thiols play an important role as thiol-cofactors for many enzymes and are crucial to maintain the reduced state of the cytoplasm. Most Gram-negative bacteria utilize glutathione (GSH) as major LMW thiol. However, in Gram-positive Actinomycetes and Firmicutes alternative LMW thiols, such as mycothiol (MSH) and bacillithiol (BSH) play related roles as GSH surrogates, respectively. Under conditions of hypochlorite stress, MSH and BSH are known to form mixed disulfides with protein thiols, termed as S-mycothiolation or S-bacillithiolation that function in thiol-protection and redox regulation. Protein S-thiolations are widespread redox-modifications discovered in different Gram-positive bacteria, such as Bacillus and Staphylococcus species, Mycobacterium smegmatis, Corynebacterium glutamicum and Corynebacterium diphtheriae. S-thiolated proteins are mainly involved in cellular metabolism, protein translation, redox regulation and antioxidant functions with some conserved targets across bacteria. The reduction of protein S-mycothiolations and S-bacillithiolations requires glutaredoxin-related mycoredoxin and bacilliredoxin pathways to regenerate protein functions. In this review, we present an overview of the functions of mycothiol and bacillithiol and their physiological roles in protein S-bacillithiolations and S-mycothiolations in Gram-positive bacteria. Significant progress has been made to characterize the role of protein S-thiolation in redox-regulation and thiol protection of main metabolic and antioxidant enzymes. However, the physiological roles of the pathways for regeneration are only beginning to emerge as well as their interactions with other cellular redox systems. Future studies should be also directed to explore the roles of protein S-thiolations and their redox pathways in pathogenic bacteria under infection conditions to discover new drug targets and treatment options against multiple antibiotic resistant bacteria. |
format | Online Article Text |
id | pubmed-6178380 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | Elsevier |
record_format | MEDLINE/PubMed |
spelling | pubmed-61783802018-10-11 Redox regulation by reversible protein S-thiolation in Gram-positive bacteria Imber, Marcel Pietrzyk-Brzezinska, Agnieszka J. Antelmann, Haike Redox Biol Review Article Low molecular weight (LMW) thiols play an important role as thiol-cofactors for many enzymes and are crucial to maintain the reduced state of the cytoplasm. Most Gram-negative bacteria utilize glutathione (GSH) as major LMW thiol. However, in Gram-positive Actinomycetes and Firmicutes alternative LMW thiols, such as mycothiol (MSH) and bacillithiol (BSH) play related roles as GSH surrogates, respectively. Under conditions of hypochlorite stress, MSH and BSH are known to form mixed disulfides with protein thiols, termed as S-mycothiolation or S-bacillithiolation that function in thiol-protection and redox regulation. Protein S-thiolations are widespread redox-modifications discovered in different Gram-positive bacteria, such as Bacillus and Staphylococcus species, Mycobacterium smegmatis, Corynebacterium glutamicum and Corynebacterium diphtheriae. S-thiolated proteins are mainly involved in cellular metabolism, protein translation, redox regulation and antioxidant functions with some conserved targets across bacteria. The reduction of protein S-mycothiolations and S-bacillithiolations requires glutaredoxin-related mycoredoxin and bacilliredoxin pathways to regenerate protein functions. In this review, we present an overview of the functions of mycothiol and bacillithiol and their physiological roles in protein S-bacillithiolations and S-mycothiolations in Gram-positive bacteria. Significant progress has been made to characterize the role of protein S-thiolation in redox-regulation and thiol protection of main metabolic and antioxidant enzymes. However, the physiological roles of the pathways for regeneration are only beginning to emerge as well as their interactions with other cellular redox systems. Future studies should be also directed to explore the roles of protein S-thiolations and their redox pathways in pathogenic bacteria under infection conditions to discover new drug targets and treatment options against multiple antibiotic resistant bacteria. Elsevier 2018-08-24 /pmc/articles/PMC6178380/ /pubmed/30308476 http://dx.doi.org/10.1016/j.redox.2018.08.017 Text en © 2018 The Authors http://creativecommons.org/licenses/by-nc-nd/4.0/ This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/). |
spellingShingle | Review Article Imber, Marcel Pietrzyk-Brzezinska, Agnieszka J. Antelmann, Haike Redox regulation by reversible protein S-thiolation in Gram-positive bacteria |
title | Redox regulation by reversible protein S-thiolation in Gram-positive bacteria |
title_full | Redox regulation by reversible protein S-thiolation in Gram-positive bacteria |
title_fullStr | Redox regulation by reversible protein S-thiolation in Gram-positive bacteria |
title_full_unstemmed | Redox regulation by reversible protein S-thiolation in Gram-positive bacteria |
title_short | Redox regulation by reversible protein S-thiolation in Gram-positive bacteria |
title_sort | redox regulation by reversible protein s-thiolation in gram-positive bacteria |
topic | Review Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6178380/ https://www.ncbi.nlm.nih.gov/pubmed/30308476 http://dx.doi.org/10.1016/j.redox.2018.08.017 |
work_keys_str_mv | AT imbermarcel redoxregulationbyreversibleproteinsthiolationingrampositivebacteria AT pietrzykbrzezinskaagnieszkaj redoxregulationbyreversibleproteinsthiolationingrampositivebacteria AT antelmannhaike redoxregulationbyreversibleproteinsthiolationingrampositivebacteria |