The aconitase of Sulfolobus solfataricus, a hyperthermophilic crenarchaeon, was cloned and heterologously expressed in Escherichia coli. Enzymic analyses and EPR measurements indicated clearly that the iron-sulphur cluster of the thermophilic aconitase was already inserted in the mesophilic host. The enzyme was purified to a specific activity of approx.44 units/mg and to 90% homogeneity. The enzymic parameters of the recombinant aconitase turned out to be in the same range as the respective values for the previously characterized native enzyme from the closely related S. acidocaldarius. Based on its primary sequence, the recombinant aconitase is closely related to bacterial A-like and to eukaryotic iron regulatory protein-like proteins. Specific aconitase activities in cytosolic extracts of S. acidocaldarius were found to be decreased markedly in iron-starved compared with iron-repleted cells. However, no differences in aconitase levels between iron-starved and iron-supplemented cells could be detected by immunostaining.
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Conference Article|
August 01 2002
Sulfolobus aconitase, a regulator of iron metabolism?
H. Uhrigshardt;
H. Uhrigshardt
1Institute of Biochemistry, University of Lübeck, Ratzeburger Allee 160, D-23538 Lübeck, Germany
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S. Zoske;
S. Zoske
1Institute of Biochemistry, University of Lübeck, Ratzeburger Allee 160, D-23538 Lübeck, Germany
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S. Anemüller
S. Anemüller
1
1Institute of Biochemistry, University of Lübeck, Ratzeburger Allee 160, D-23538 Lübeck, Germany
1 To whom correspondence should be addressed (e-mail anemueller@biochem.mu-luebeck.de)
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Publisher: Portland Press Ltd
Received:
March 12 2002
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© 2002 Biochemical Society
2002
Biochem Soc Trans (2002) 30 (4): 685–687.
Article history
Received:
March 12 2002
Citation
H. Uhrigshardt, S. Zoske, S. Anemüller; Sulfolobus aconitase, a regulator of iron metabolism?. Biochem Soc Trans 1 August 2002; 30 (4): 685–687. doi: https://doi.org/10.1042/bst0300685
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