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Phenylalanine ammonia‐lyase and cinnamate 4‐hydroxylase genes' response to HHO in E upatorium adenophorum
Author(s) -
Pei Xixiang,
Guo Huiming,
Wan Fanghao,
Cheng Hongmei
Publication year - 2012
Publication title -
weed biology and management
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.351
H-Index - 36
eISSN - 1445-6664
pISSN - 1444-6162
DOI - 10.1111/j.1445-6664.2012.00450.x
Subject(s) - phenylalanine ammonia lyase , eupatorium , biology , gene , phenylalanine , allelopathy , enzyme , biochemistry , botany , amino acid , germination
6‐ H ydroxy‐5‐isopropyl‐3,8‐dimethyl‐4a,5,6,7,8,8a‐hexahydronaphthalen‐2(1 H )‐one ( HHO ) is an allelopathic substance that is related to allelochemical metabolism in Eupatorium adenophorum . In this study, the full‐length complementary DNA of two phenylalanine ammonia‐lyase ( PAL ) genes and a fragment of the cinnamate 4‐hydroxylase ( CA4H ) gene from E . adenophorum ( E a) were cloned. The expression of all three genes was increased by the HHO treatment, with varying sensitivity: EaPAL2 > EaPAL1 > EaCA4H . Southern blotting suggested that there is a third member of the PAL gene family in this species.