scholarly journals Dimers of glutaredoxin 2 as mitochondrial redox sensors in selenite-induced oxidative stress

Metallomics ◽  
2019 ◽  
Vol 11 (7) ◽  
pp. 1241-1251 ◽  
Author(s):  
Valeria Scalcon ◽  
Federica Tonolo ◽  
Alessandra Folda ◽  
Alberto Bindoli ◽  
Maria Pia Rigobello
Keyword(s):  
Oxidative Stress ◽  
Iron Release ◽  
Iron Sulfur Cluster ◽  
Sulfur Cluster ◽  
Iron Sulfur ◽  
Redox Sensors

Grx2 coordinates an iron–sulfur cluster, forming inactive dimers. In mitochondria, Grx2 monomerization, after oxidative stress, determines iron release triggering apoptosis.

scholarly journals The iron-sulfur cluster assembly network component NARFL is a key element in the cellular defense against oxidative stress

2015 ◽  
Vol 89 ◽  
pp. 863-872 ◽  
Author(s):  
Monique V. Corbin ◽  
Davy A.P. Rockx ◽  
Anneke B. Oostra ◽  
Hans Joenje ◽  
Josephine C. Dorsman
Keyword(s):  
Oxidative Stress ◽  
Cluster Assembly ◽  
Iron Sulfur Cluster ◽  
Sulfur Cluster ◽  
Cellular Defense ◽  
Iron Sulfur ◽  
Network Component

The cysteine desulfurase IscS of Mycobacterium tuberculosis is involved in iron–sulfur cluster biogenesis and oxidative stress defence

2014 ◽  
Vol 459 (3) ◽  
pp. 467-478 ◽  
Author(s):  
Jan Rybniker ◽  
Florence Pojer ◽  
Jan Marienhagen ◽  
Gaëlle S. Kolly ◽  
Jeffrey M. Chen ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Mycobacterium Tuberculosis ◽  
Interaction Network ◽  
Cluster Assembly ◽  
Cysteine Desulfurase ◽  
Iron Sulfur Cluster ◽  
Sulfur Cluster ◽  
Iron Sulfur ◽  
Altered Surface ◽  
Made In

IscS of Mycobacterium tuberculosis is an essential component of iron–sulfur cluster assembly conferring resistance to oxidative stress. The strongly altered surface structure and the extensive protein-interaction network identified in the present study mirrors adaptations made in response to a heavily depleted mycobacterial ISC operon.

scholarly journals Cysteine Deprivation Targets Ovarian Clear Cell Carcinoma Via Oxidative Stress and Iron−Sulfur Cluster Biogenesis Deficit

2020 ◽  
Vol 33 (17) ◽  
pp. 1191-1208 ◽  
Author(s):  
Wisna Novera ◽  
Zheng-Wei Lee ◽  
Dawn Sijin Nin ◽  
Melvin Zi-Yu Dai ◽  
Shabana Binte Idres ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Cell Carcinoma ◽  
Clear Cell ◽  
Clear Cell Carcinoma ◽  
Ovarian Clear Cell Carcinoma ◽  
Iron Sulfur Cluster ◽  
Sulfur Cluster ◽  
Iron Sulfur

scholarly journals Oxidative stress enhances the expression of sulfur assimilation genes: preliminary insights on the Enterococcus faecalis iron-sulfur cluster machinery regulation

2014 ◽  
Vol 109 (4) ◽  
pp. 408-413 ◽  
Author(s):  
Gustavo Pelicioli Riboldi ◽  
Christine Garcia Bierhals ◽  
Eduardo Preusser de Mattos ◽  
Ana Paula Guedes Frazzon ◽  
Pedro Alves d?Azevedo ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Enterococcus Faecalis ◽  
Sulfur Assimilation ◽  
Iron Sulfur Cluster ◽  
Sulfur Cluster ◽  
Iron Sulfur

scholarly journals Iron-sulfur clusters are involved in post-translational arginylation

2021 ◽  
Author(s):  
Verna Van ◽  
Janae B. Brown ◽  
Hannah Rosenbach ◽  
Ijaz Mohamed ◽  
Nna-Emeka Ejimogu ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Molecular Mechanism ◽  
Half Life ◽  
Regulatory Control ◽  
Post Translational Modification ◽  
Iron Sulfur Cluster ◽  
Iron Sulfur Clusters ◽  
Sulfur Cluster ◽  
Iron Sulfur ◽  
Oxygen Sensitive

Eukaryotic arginylation is an essential post-translational modification that both modulates protein stability and regulates protein half-life through the N-degron pathway. Arginylation is catalyzed by a family of enzymes known as the arginyl-tRNA transferases (ATE1s), which are conserved across the eukaryotic domain. Despite its conservation and importance, little is known regarding the structure, mechanism, and regulation of ATE1s. In this work, we have discovered that ATE1s bind a previously unknown iron-sulfur cluster that is conserved across evolution. We have extensively characterized the nature of this iron-sulfur cluster, and we show that the presence of the iron-sulfur cluster is linked to alterations in arginylation efficacy. Finally, we demonstrate that the ATE1 iron-sulfur cluster is oxygen sensitive, which could be a molecular mechanism of the N-degron pathway to sense oxidative stress. Thus, our data provide the framework of a cluster-based paradigm of ATE1 regulatory control.

scholarly journals Cysteine Desulfurase IscS2 Plays a Role in Oxygen Resistance in Clostridium difficile

2018 ◽  
Vol 86 (8) ◽  
Author(s):  
Nicole Giordano ◽  
Jessica L. Hastie ◽  
Ashley D. Smith ◽  
Elissa D. Foss ◽  
Daniela F. Gutierrez-Munoz ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Clostridium Difficile ◽  
The United States ◽  
Growth Defect ◽  
Cysteine Desulfurase ◽  
Iron Sulfur Cluster ◽  
Content Type ◽  
Sulfur Cluster ◽  
Iron Sulfur ◽  
Low Levels

ABSTRACT Clostridium difficile is an anaerobic, spore-forming bacterium capable of colonizing the gastrointestinal tract of humans following disruption of the normal microbiota, typically from antibiotic therapy for an unrelated infection. With approximately 500,000 confirmed infections leading to 29,000 deaths per year in the United States, C. difficile infection (CDI) is an urgent public health threat. We previously determined that C. difficile survives in up to 3% oxygen. Low levels of oxygen are present in the intestinal tract, with the higher concentrations being associated with the epithelial cell surface. Additionally, antibiotic treatment, the greatest risk factor for CDI, increases the intestinal oxygen concentration. Therefore, we hypothesized that the C. difficile genome encodes mechanisms for survival during oxidative stress. Previous data have shown that cysteine desulfurases involved in iron-sulfur cluster assembly are involved in protecting bacteria from oxidative stress. In this study, deletion of a putative cysteine desulfurase (Cd630_12790/IscS2) involved in the iron-sulfur cluster (Isc) system caused a severe growth defect in the presence of 2% oxygen. Additionally, this mutant delayed colonization in a conventional mouse model of CDI and failed to colonize in a germfree model, which has higher intestinal oxygen levels. These data imply an undefined role for this cysteine desulfurase in protecting C. difficile from low levels of oxygen in the gut.

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