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dc.contributor.author Qi, Xiaoquan
dc.contributor.author Bakht, Saleha
dc.contributor.author Qin, Bo
dc.contributor.author Leggett, J. Michael
dc.contributor.author Hemmings, Andrew
dc.contributor.author Mellon, Fred
dc.contributor.author Eagles, John
dc.contributor.author Werck-Reichhart, Daniele
dc.contributor.author Schaller, Hubert
dc.contributor.author Lesot, Agnes
dc.contributor.author Melton, Rachel
dc.contributor.author Osbourn, Anne
dc.date.accessioned 2009-07-21T13:58:02Z
dc.date.available 2009-07-21T13:58:02Z
dc.date.issued 2006
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
dc.identifier.other PURE: 112653
dc.identifier.other dspace: 2160/2693
dc.identifier.uri http://hdl.handle.net/2160/2693
dc.identifier.uri http://www.pnas.org/cgi/content/full/103/49/18848 en
dc.description 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, 103, (49), 18848-18853. Sponsorship: BBSRC; Gatsby Charitable Foundation en
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
dc.format.extent 6 en
dc.language.iso eng
dc.relation.ispartof Proceedings of the National Academy of Sciences of the United States of America en
dc.subject Avena en
dc.subject disease resistance en
dc.subject oat en
dc.subject metabolic diversity en
dc.subject gene duplication en
dc.title A different function for a member of an ancient and highly conserved cytochrome P450 family: From essential sterols to plant defense en
dc.type Text en
dc.type.publicationtype Article (Journal) en
dc.identifier.doi http://dx.doi.org/10.1073/pnas.0607849103
dc.contributor.institution Aberystwyth University en
dc.contributor.institution Institute of Biological, Environmental and Rural Sciences en
dc.description.status Peer reviewed en


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