The N-Terminus of Iron–Sulfur Cluster Assembly Factor ISD11 Is Crucial for Subcellular Targeting and Interaction with l-Cysteine Desulfurase NFS1

Biochemistry ◽  
2017 ◽  
Vol 56 (12) ◽  
pp. 1797-1808 ◽  
Author(s):  
Martin Friemel ◽  
Zvonimir Marelja ◽  
Kuanyu Li ◽  
Silke Leimkühler
Keyword(s):  
Cluster Assembly ◽  
Subcellular Targeting ◽  
Cysteine Desulfurase ◽  
Iron Sulfur Cluster ◽  
Sulfur Cluster ◽  
Iron Sulfur ◽  
N Terminus ◽  
Assembly Factor

Biogenesis and Transfer of Iron-Sulfur Clusters from Acidithiobacillus ferrooxidans

2013 ◽  
Vol 825 ◽  
pp. 198-201 ◽  
Author(s):  
Jian She Liu ◽  
Lin Qian ◽  
Chun Li Zheng
Keyword(s):  
Acidithiobacillus Ferrooxidans ◽  
Binding Protein ◽  
Cluster Assembly ◽  
Cysteine Desulfurase ◽  
Iron Sulfur Cluster ◽  
Iron Sulfur Clusters ◽  
Sulfur Cluster ◽  
Iron Sulfur ◽  
Iron Sulfur Proteins

Iron-sulfur (Fe-S) proteins are ubiquitous and participate in multiple essential functions of life. However, little is currently known about the mechanisms of iron-sulfur biosynthesis and transfer in acidophilic microorganisms. In this study, the IscS, IscU and IscA proteins from Acidithiobacillus ferrooxidans were successfully expressed in Escherichia coli and purified by affinity chromatography. The IscS was a cysteine desulfurase which catalyzes desulfurization of L-cysteine and transfer sulfur for iron-sulfur cluster assembly. Purified IscU did not have an iron-sulfur cluster but could act as a scaffold protein to assemble the [2Fe-2S] cluster in vitro. The IscA was a [4Fe-4S] cluster binding protein, but it also acted as an iron binding protein. Further studies indicated that the iron sulfur clusters could be transferred from pre-assembled scaffold proteins to apo-form iron sulfur proteins, the reconstituted iron sulfur proteins could restore their physiological activities.

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 Multiple Sense and Antisense Promoters Contribute to the Regulated Expression of the isc-suf Operon for Iron-Sulfur Cluster Assembly in Rhodobacter

2019 ◽  
Vol 7 (12) ◽  
pp. 671 ◽  
Author(s):  
Xin Nie ◽  
Bernhard Remes ◽  
Gabriele Klug
Keyword(s):  
Rhodobacter Sphaeroides ◽  
Photosynthetic Electron Transport ◽  
Regulatory Proteins ◽  
Cluster Assembly ◽  
Iron Sulfur Cluster ◽  
Iron Sulfur Clusters ◽  
Sulfur Cluster ◽  
Iron Sulfur ◽  
Photosynthetic Complexes ◽  
The One

A multitude of biological functions relies on iron-sulfur clusters. The formation of photosynthetic complexes goes along with an additional demand for iron-sulfur clusters for bacteriochlorophyll synthesis and photosynthetic electron transport. However, photooxidative stress leads to the destruction of iron-sulfur clusters, and the released iron promotes the formation of further reactive oxygen species. A balanced regulation of iron-sulfur cluster synthesis is required to guarantee the supply of this cofactor, on the one hand, but also to limit stress, on the other hand. The phototrophic alpha-proteobacterium Rhodobacter sphaeroides harbors a large operon for iron-sulfur cluster assembly comprising the iscRS and suf genes. IscR (iron-sulfur cluster regulator) is an iron-dependent regulator of isc-suf genes and other genes with a role in iron metabolism. We applied reporter gene fusions to identify promoters of the isc-suf operon and studied their activity alone or in combination under different conditions. Gel-retardation assays showed the binding of regulatory proteins to individual promoters. Our results demonstrated that several promoters in a sense and antisense direction influenced isc-suf expression and the binding of the IscR, Irr, and OxyR regulatory proteins to individual promoters. These findings demonstrated a complex regulatory network of several promoters and regulatory proteins that helped to adjust iron-sulfur cluster assembly to changing conditions in Rhodobacter sphaeroides.

scholarly journals Regulation of the HscA ATPase Reaction Cycle by the Co-chaperone HscB and the Iron-Sulfur Cluster Assembly Protein IscU

2004 ◽  
Vol 279 (52) ◽  
pp. 53924-53931 ◽  
Author(s):  
Jonathan J. Silberg ◽  
Tim L. Tapley ◽  
Kevin G. Hoff ◽  
Larry E. Vickery
Keyword(s):  
Cluster Assembly ◽  
Iron Sulfur Cluster ◽  
Reaction Cycle ◽  
Sulfur Cluster ◽  
Iron Sulfur ◽  
Atpase Reaction
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