Expression, purification and characterization of an iron-sulfur cluster assembly protein, IscU, from Acidithiobacillus ferrooxidans

2007 ◽  
Vol 29 (12) ◽  
pp. 1965-1972 ◽  
Author(s):  
Jia Zeng ◽  
Wenjie Zhao ◽  
Yuandong Liu ◽  
Lexian Xia ◽  
Jianshe Liu ◽  
...  
2007 ◽  
Vol 20-21 ◽  
pp. 509-512 ◽  
Author(s):  
Jian She Liu ◽  
Yan Fei Zhang ◽  
Mei Mei Geng ◽  
Jia Zeng ◽  
Guan Zhou Qiu

The highly conserved operon iron–sulfur cluster (iscSUA) is essential for the general biogenesis and transfer of iron–sulfur proteins in bacteria. In this study, expression, purification and characterization of the proteins of the isc operon (iscSUA) of Acidithiobacillus ferrooxidans ATCC 23270 was studied. Assembly and transfer of [Fe4S4] in vitro during the isc proteins and other iron sulfur proteins was studied in order to detect the pathway and mechanism of [Fe4S4] assembly and transfer in vivo. The [Fe4S4] cluster was successfully assembled in iron-sulfur proteins in vitro in the presence of Fe2+ and sulfide, and it was successfully transferred from IscA or IscU to iron- sulfur proteins. Our results support and extend certain models of iron-sulfur clusters assembly and transfer.


Gene ◽  
2016 ◽  
Vol 585 (1) ◽  
pp. 159-165 ◽  
Author(s):  
Zarna Rajeshkumar Pala ◽  
Vishal Saxena ◽  
Gagandeep Singh Saggu ◽  
Sushil Kumar Yadav ◽  
R.P. Pareek ◽  
...  

2013 ◽  
Vol 825 ◽  
pp. 198-201 ◽  
Author(s):  
Jian She Liu ◽  
Lin Qian ◽  
Chun Li Zheng

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.


Biochemistry ◽  
2002 ◽  
Vol 41 (15) ◽  
pp. 5024-5032 ◽  
Author(s):  
Gong Wu ◽  
Sheref S. Mansy ◽  
Shu-pao Wu ◽  
Kristene K. Surerus ◽  
Matthew W. Foster ◽  
...  

2005 ◽  
Vol 59 (4) ◽  
pp. 875-881 ◽  
Author(s):  
Jinyu Liu ◽  
Natalia Oganesyan ◽  
Dong-Hae Shin ◽  
Jarmila Jancarik ◽  
Hisao Yokota ◽  
...  

2000 ◽  
Vol 64 (11) ◽  
pp. 2412-2419 ◽  
Author(s):  
Shin-ichiro KATO ◽  
Hisaaki MIHARA ◽  
Tatsuo KURIHARA ◽  
Tohru YOSHIMURA ◽  
Nobuyoshi ESAKI

2006 ◽  
Vol 63 (4) ◽  
pp. 1137-1137
Author(s):  
Jinyu Liu ◽  
Natalia Oganesyan ◽  
Dong-Hae Shin ◽  
Jarmila Jancarik ◽  
Hisao Yokota ◽  
...  

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