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dc.contributor.author Xiaoquan en_US
dc.contributor.author Saleha en_US
dc.contributor.author Bo en_US
dc.contributor.author J. Michael en_US
dc.contributor.author Andrew en_US
dc.contributor.author Fred en_US
dc.contributor.author John en_US
dc.contributor.author Daniele en_US
dc.contributor.author Hubert en_US
dc.contributor.author Agnes en_US
dc.contributor.author Rachel en_US
dc.contributor.author Anne en_US
dc.date.accessioned 2009-07-21T13:58:02Z
dc.date.available 2009-07-21T13:58:02Z
dc.date.issued 2006 en_US
dc.identifier http://dx.doi.org/10.1073/pnas.0607849103 en_US
dc.identifier.citation Qi , X , Bakht , S , Qin , B , Leggett , J M , Hemmings , A , Mellon , F , Eagles , J , Werck-Reichhart , D , Schaller , H , Lesot , A , Melton , R & Osbourn , A 2006 , ' A different function for a member of an ancient and highly conserved cytochrome P450 family: From essential sterols to plant defense ' Proceedings of the National Academy of Sciences of the United States of America , vol 103 , no. 49 , pp. 18848-18853 . , 10.1073/pnas.0607849103 en_US
dc.identifier.other PURE: 112653 en_US
dc.identifier.other dspace: 2160/2693 en_US
dc.identifier.uri http://hdl.handle.net/2160/2693
dc.description.abstract CYP51 sterol demethylases are the only cytochrome P450 enzymes with a conserved function across the animal, fungal, and plant kingdoms (in the synthesis of essential sterols). These highly conserved enzymes, which are important targets for cholesterol-lowering drugs, antifungal agents, and herbicides, are regarded as the most ancient member cytochrome P450 family. Here we present a report of a CYP51 enzyme that has acquired a different function. We show that the plant enzyme AsCYP51H10 is dispensable for synthesis of essential sterols and has been recruited for the production of antimicrobial compounds (avenacins) that confer disease resistance in oats. The AsCyp51H10 gene is synonymous with Sad2, a gene that we previously had defined by mutation as being required for avenacin synthesis. In earlier work, we showed that Sad1, the gene encoding the first committed enzyme in the avenacin pathway (β-amyrin synthase), had arisen by duplication and divergence of a cycloartenol synthase-like gene. Together these data indicate an intimate evolutionary connection between the sterol and avenacin pathways. Sad1 and Sad2 lie within 70 kb of each other and are expressed specifically in the epidermal cells of the root tip, the site of accumulation of avenacins. These findings raise intriguing questions about the recruitment, coevolution, and regulation of the components of this specialized defense-related metabolic pathway. en_US
dc.format.extent 6 en_US
dc.relation.ispartof Proceedings of the National Academy of Sciences of the United States of America en_US
dc.subject Avena en_US
dc.subject disease resistance en_US
dc.subject oat en_US
dc.subject metabolic diversity en_US
dc.subject gene duplication en_US
dc.title A different function for a member of an ancient and highly conserved cytochrome P450 family: From essential sterols to plant defense en_US
dc.contributor.pbl Aberystwyth University en_US
dc.contributor.pbl Institute of Biological, Environmental and Rural Sciences en_US


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