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ARS Home » Midwest Area » Lexington, Kentucky » Forage-animal Production Research » Research » Publications at this Location » Publication #231880
Title: Role of the LolP Cytochrome P450 Monooxygenase in Loline Alkaloid Biosynthesis

Author
item SPIERING, MARTIN - UNIVERSITY OF KENTUCKY
item FAULKNER, JEROME - UNIVERSITY OF KENTUCKY
item ZHANG, DONG-XIU - UNIVERSITY OF KENTUCKY
item MACHADO, CAROLINE - UNIVERSITY OF KENTUCKY
item GROSSMAN, ROBERT - UNIVERSITY OF KENTUCKY
item SCHARDL, CHRISTOPHER - UNIVERSITY OF KENTUCKY

Submitted to: Fungal Genetics and Biology
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 7/7/2008
Publication Date: 7/7/2008
Citation: Spiering, M.J., Faulkner, J.R., Zhang, D., Machado, C., Grossman, R.B., Schardl, C.L. 2008. Role of the LolP Cytochrome P450 Monooxygenase in Loline Alkaloid Biosynthesis. Fungal Genetics and Biology. 45:1307-1314.

Interpretive Summary: University of Kentucky publication funded via a congressionally mandated SCA entitled "Continuation of Improved Forage Livestock Production System (CRIS Number: 6440-21310-002-05S)".

Technical Abstract: The insecticidal loline alkaloids, produced by Neotyphodium uncinatum and related endophytes, are exo-1-aminopyrrolizidines with an ether bridge between C-2 and C-7. Loline alkaloids vary in methyl, acetyl, and formyl substituents on the 1-amine, which affect their biological activity. Enzymes for key loline biosynthesis steps are probably encoded by genes in the LOL cluster, which is duplicated in N. uncinatum, except for a large deletion in lolP2. The role of lolP1 was investigated by its replacement wit ha hygromycin B phosphotransferase gene. Compared to wild type N. uncinatum and an ectopic transformant. 'lolP1 cultures had greatly elevated levels of N-mythylloline (NML) and lacked N-formylloline (NFL). Complementation of 'lolP1 with lolP1 under control of the Emericella nidulans trpC promoter restored NFL production. These results and the inferred sequence of LolP1 indicate that it is a cytochrome P450, catalyzing oxygenation of an N-methyl group in NML to the N-formyl group in NFL.