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Three 4‐coumarate:coenzyme A ligases in Arabidopsis thaliana represent two evolutionarily divergent classes in angiosperms
Author(s) -
Ehlting Jürgen,
Büttner Daniela,
Wang Qing,
Douglas Carl J.,
Somssich Imre E.,
Kombrink Erich
Publication year - 1999
Publication title -
the plant journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.058
H-Index - 269
eISSN - 1365-313X
pISSN - 0960-7412
DOI - 10.1046/j.1365-313x.1999.00491.x
Subject(s) - arabidopsis thaliana , biology , arabidopsis , phenylpropanoid , gene , gene family , biochemistry , genetics , biosynthesis , gene expression , mutant
Summary The enzyme 4‐coumarate:CoA ligase (4CL) plays a key role in channelling carbon flow into diverse branch pathways of phenylpropanoid metabolism which serve important functions in plant growth and adaptation to environmental perturbations. Here we report on the cloning of the 4CL gene family from Arabidopsis thaliana and demonstrate that its three members, At4CL1 , At4CL2 and At4CL3 , encode isozymes with distinct substrate preference and specificities. Expression studies revealed a differential behaviour of the three genes in various plant organs and upon external stimuli such as wounding and UV irradiation or upon challenge with the fungus, Peronospora parasitica . Phylogenetic comparisons indicate that, in angiosperms, 4CL can be classified into two major clusters, class I and class II, with the At 4CL1 and At 4CL2 isoforms belonging to class I and At 4CL3 to class II. Based on their enzymatic properties, expression characteristics and evolutionary relationships, At 4CL3 is likely to participate in the biosynthetic pathway leading to flavonoids whereas At 4CL1 and At 4CL2 are probably involved in lignin formation and in the production of additional phenolic compounds other than flavonoids.