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Download Hi-Res ImageDownload to MS-PowerPointCite This:Biochemistry 2013, 52, 18, 3041-3050
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A Radical Transfer Pathway in Spore Photoproduct Lyase

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† Department of Chemistry and Chemical Biology, Indiana University-Purdue University Indianapolis, Indianapolis, Indiana 46202, United States
‡ Department of Biological, Chemical, and Physical Sciences, Roosevelt University, Chicago, Illinois 60605, United States
§ Department of Chemistry, University of Washington, Seattle, Washington 98195, United States
∥ Department of Biomolecular Mechanisms, Max-Planck Institute for Medical Research, Jahnstrasse 29, 69120 Heidelberg, Germany
*A.B.: Department of Biomolecular Mechanisms, Max-Planck Institute for Medical Research, Jahnstrasse 29, 69120 Heidelberg, Germany; telephone, +49 6221 486 515; fax, +49 6221 486 585; e-mail, [email protected]. S.S.: Department of Chemistry, University of Washington, Seattle, WA 98195; telephone, (206) 543-2906; e-mail, [email protected]. L.L.: Department of Chemistry and Chemistry Biology, Indiana University-Purdue University Indianapolis, 402 N. Blackford Street, LD 326, Indianapolis, IN 46202; telephone, (317) 278-2202; fax, (317) 274-4701; e-mail, [email protected]
Cite this: Biochemistry 2013, 52, 18, 3041–3050
Publication Date (Web):April 15, 2013
https://doi.org/10.1021/bi3016247
Copyright © 2013 American Chemical Society
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    Abstract

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    Spore photoproduct lyase (SPL) repairs a covalent UV-induced thymine dimer, spore photoproduct (SP), in germinating endospores and is responsible for the strong UV resistance of endospores. SPL is a radical S-adenosyl-l-methionine (SAM) enzyme, which uses a [4Fe-4S]+ cluster to reduce SAM, generating a catalytic 5′-deoxyadenosyl radical (5′-dA•). This in turn abstracts a H atom from SP, generating an SP radical that undergoes β scission to form a repaired 5′-thymine and a 3′-thymine allylic radical. Recent biochemical and structural data suggest that a conserved cysteine donates a H atom to the thymine radical, resulting in a putative thiyl radical. Here we present structural and biochemical data that suggest that two conserved tyrosines are also critical in enzyme catalysis. One [Y99(Bs) in Bacillus subtilis SPL] is downstream of the cysteine, suggesting that SPL uses a novel hydrogen atom transfer (HAT) pathway with a pair of cysteine and tyrosine residues to regenerate SAM. The other tyrosine [Y97(Bs)] has a structural role to facilitate SAM binding; it may also contribute to the SAM regeneration process by interacting with the putative •Y99(Bs) and/or 5′-dA• intermediates to lower the energy barrier for the second H abstraction step. Our results indicate that SPL is the first member of the radical SAM superfamily (comprising more than 44000 members) to bear a catalytically operating HAT chain.

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