In Vitro Studies of Cellular Iron–Sulfur Cluster Biosynthesis, Trafficking, and Transport

2017 ◽  
pp. 55-82 ◽  
Author(s):  
Christine Wachnowsky ◽  
James A. Cowan
Keyword(s):  
In Vitro Studies ◽  
Iron Sulfur Cluster ◽  
Sulfur Cluster ◽  
Cellular Iron ◽  
Iron Sulfur ◽  
Cluster Biosynthesis

scholarly journals Evolutionary conservation and in vitro reconstitution of microsporidian iron–sulfur cluster biosynthesis

2017 ◽  
Vol 8 (1) ◽  
Author(s):  
Sven-A. Freibert ◽  
Alina V. Goldberg ◽  
Christian Hacker ◽  
Sabine Molik ◽  
Paul Dean ◽  
...  
Keyword(s):  
Evolutionary Conservation ◽  
Iron Sulfur Cluster ◽  
Sulfur Cluster ◽  
Iron Sulfur ◽  
In Vitro Reconstitution ◽  
Cluster Biosynthesis

scholarly journals In Vivo Demonstration of FNR Dimers in Response to Lower O2 Availability

2007 ◽  
Vol 189 (7) ◽  
pp. 2930-2932 ◽  
Author(s):  
Adrian J. Jervis ◽  
Jeffrey Green
Keyword(s):  
Escherichia Coli ◽  
Transcription Factor ◽  
Current Model ◽  
In Vitro Studies ◽  
Iron Sulfur Cluster ◽  
Sulfur Cluster ◽  
Iron Sulfur ◽  
Two Hybrid

ABSTRACT Escherichia coli FNR is an O2-sensing transcription factor. In vitro studies indicate that anaerobic iron-sulfur cluster acquisition promotes FNR dimerization. Here, two-hybrid assays show that iron-sulfur cluster-dependent FNR dimers are formed in vivo in response to lower O2 availability, consistent with the current model of FNR activation.

scholarly journals Two plant-derived aporphinoid alkaloids exert their antifungal activity by disrupting mitochondrial iron-sulfur cluster biosynthesis

2017 ◽  
Vol 292 (40) ◽  
pp. 16578-16593 ◽  
Author(s):  
Siddharth K. Tripathi ◽  
Tao Xu ◽  
Qin Feng ◽  
Bharathi Avula ◽  
Xiaomin Shi ◽  
...  
Keyword(s):  
Antifungal Activity ◽  
Iron Sulfur Cluster ◽  
Sulfur Cluster ◽  
Iron Sulfur ◽  
Mitochondrial Iron ◽  
Cluster Biosynthesis

scholarly journals Iron–sulfur cluster biosynthesis

2008 ◽  
Vol 36 (6) ◽  
pp. 1112-1119 ◽  
Author(s):  
Sibali Bandyopadhyay ◽  
Kala Chandramouli ◽  
Michael K. Johnson
Keyword(s):  
Scaffold Proteins ◽  
Cluster Assembly ◽  
Cysteine Desulfurase ◽  
Iron Sulfur Cluster ◽  
Iron Sulfur ◽  
Eukaryotic Organisms ◽  
Almost All ◽  
Cluster Biosynthesis

Iron–sulfur (Fe–S) clusters are present in more than 200 different types of enzymes or proteins and constitute one of the most ancient, ubiquitous and structurally diverse classes of biological prosthetic groups. Hence the process of Fe–S cluster biosynthesis is essential to almost all forms of life and is remarkably conserved in prokaryotic and eukaryotic organisms. Three distinct types of Fe–S cluster assembly machinery have been established in bacteria, termed the NIF, ISC and SUF systems, and, in each case, the overall mechanism involves cysteine desulfurase-mediated assembly of transient clusters on scaffold proteins and subsequent transfer of pre-formed clusters to apo proteins. A molecular level understanding of the complex processes of Fe–S cluster assembly and transfer is now beginning to emerge from the combination of in vivo and in vitro approaches. The present review highlights recent developments in understanding the mechanism of Fe–S cluster assembly and transfer involving the ubiquitous U-type scaffold proteins and the potential roles of accessory proteins such as Nfu proteins and monothiol glutaredoxins in the assembly, storage or transfer of Fe–S clusters.

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