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Report No.

Isolation and characterization of the fragrant cyclamen ${it O}$-methyltransferase involved in flower coloration

Akita, Yusuke; Kitamura, Satoshi; Hase, Yoshihiro; Narumi, Issei; Ishizaka, Hiroshi*; Kondo, Emiko*; Kameari, Naoko*; Nakayama, Masayoshi*; Tanikawa, Natsu*; Morita, Yasumasa*; Tanaka, Atsushi

Anthocyanin ${it O}$-methyltransferase (OMT) is one of the key enzymes for anthocyanin modification and flower pigmentation. We previously bred a novel red-purple-flowered fragrant cyclamen (KMrp) from the purple-flowered fragrant cyclamen "Kaori-no-mai" (KM) by ion-beam irradiation. Since the major anthocyanins in KMrp and KM petals were delphinidin 3,5-diglucoside and malvidin 3,5-diglucoside, respectively, inactivation of a methylation step in the anthocyanin biosynthetic pathway was indicated in KMrp. We isolated and compared ${it OMT}$ genes expressed in KM and KMrp petals. RT-PCR analysis revealed that ${it CkmOMT2}$ was expressed in the petals of KM but not in KMrp. Three additional ${it CkmOMT}$s with identical sequences were expressed in petals of both KM and KMrp. Genomic PCR analysis revealed that ${it CkmOMT2}$ was not amplified from the KMrp genome, indicating that ion-beam irradiation caused a loss of the entire ${it CkmOMT2}$ region in KMrp. In vitro enzyme assay demonstrated that CkmOMT2 catalyzes the 3' or 3',5' ${it O}$-methylation of the B-ring of anthocyanin substrates. These results suggest that CkmOMT2 is functional for anthocyanin methylation, and defective expression of ${it CkmOMT2}$ is responsible for changes in anthocyanin composition and flower coloration in KMrp.



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Category:Plant Sciences



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