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Permanent URL to this publication: http://dx.doi.org/10.5167/uzh-31467

Hinks, J A; Evans, M C W; De Miguel, Y; Sartori, A A; Jiricny, J; Pearl, L H (2002). An iron-sulfur cluster in the family 4 uracil-DNA glycosylases. Journal of Biological Chemistry, 277(19):16936-19640.

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Abstract

The 25-kDa Family 4 uracil-DNA glycosylase (UDG) from Pyrobaculum aerophilum has been expressed and purified in large quantities for structural analysis. In the process we observed it to be colored and subsequently found that it contained iron. Here we demonstrate that P. aerophilum UDG has an iron-sulfur center with the EPR characteristics typical of a 4Fe4S high potential iron protein. Interestingly, it does not share any sequence similarity with the classic iron-sulfur proteins, although four cysteines (which are strongly conserved in the thermophilic members of Family 4 UDGs) may represent the metal coordinating residues. The conservation of these residues in other members of the family suggest that 4Fe4S clusters are a common feature. Although 4Fe4S clusters have been observed previously in Nth/MutY DNA repair enzymes, this is the first observation of such a feature in the UDG structural superfamily. Similar to the Nth/MutY enzymes, the Family 4 UDG centers probably play a structural rather than a catalytic role.

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33 citations in Web of Science®
35 citations in Scopus®
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Item Type:Journal Article, refereed, original work
Communities & Collections:04 Faculty of Medicine > Institute of Molecular Cancer Research
07 Faculty of Science > Institute of Molecular Cancer Research
DDC:570 Life sciences; biology
Language:English
Date:2002
Deposited On:09 Jul 2010 14:20
Last Modified:05 Jul 2014 17:13
Publisher:American Society for Biochemistry and Molecular Biology
ISSN:0021-9258
Additional Information:This research was originally published in: Hinks, J A; Evans, M C W; De Miguel, Y; Sartori, A A; Jiricny, J; Pearl, L H (2002). An iron-sulfur cluster in the family 4 uracil-DNA glycosylases. Journal of Biological Chemistry, 277(19):16936-19640. © the American Society for Biochemistry and Molecular Biology.
Free access at:Publisher DOI. An embargo period may apply.
Publisher DOI:10.1074/jbc.M200668200
PubMed ID:11877410

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