TAILIEUCHUNG - Báo cáo Y học: Divergent members of a soybean (Glycine max L.) 4-coumarate:coenzyme A ligase gene family

4-Coumarate:CoA ligase (4CL) is involved in the formation of coenzyme A thioesters of hydroxycinnamic acids that are central substrates for subsequent condensation, reduction, and transfer reactions in the biosynthesis of plant phenylpropanoids. Previous studies of 4CL appear to suggest that many isoenzymes are functionally equivalent in supplying substrates to various subsequent branches of phenylpropanoid biosyntheses. In contrast, divergent members of a 4CL gene family were identified in soybean (Glycine max L.). We isolated three structurally and functionally distinct 4CL cDNAs encoding 4CL1, 4CL2, and 4CL3 and the gene Gm4CL3. A fourth cDNA encoding 4CL4 had high similarity with 4CL3 | Eur. J. Biochem. 269 1304-1315 2002 FEBS 2002 Divergent members of a soybean Glycine max L. 4-coumarate coenzyme A ligase gene family Primary structures catalytic properties and differential expression Christian Lindermayr1 Britta Meillers1 Judith Fliegmann1 Annette Uhlmann1 Friedrich Lottspeich2 Harald Meimberg3 and Jurgen Ebel1 1 Botanisches Institut der Universitat Munchen Germany 2Max-Planck-Institut fur Biochemie Martinsried Germany 3Institut fur Systematische Botanik der Universitat Mimchen Germany 4-Coumarate CoA ligase 4CL is involved in the formation of coenzyme A thioesters of hydroxycinnamic acids that are central substrates for subsequent condensation reduction and transfer reactions in the biosynthesis of plant phenyl-propanoids. Previous studies of 4CL appear to suggest that many isoenzymes are functionally equivalent in supplying substrates to various subsequent branches of phenylpropa-noid biosyntheses. In contrast divergent members of a 4CL gene family were identified in soybean Glycine max L. . We isolated three structurally and functionally distinct 4CL cDNAs encoding 4CL1 4CL2 and 4CL3 and the gene Gm4CL3. A fourth cDNA encoding 4CL4 had high similarity with 4CL3. The recombinant proteins expressed in Escherichia coli possessed highly divergent catalytic efficiency with various hydroxycinnamic acids. Remarkably one isoenzyme 4CL1 was able to convert sinapate thus the first cDNA encoding a 4CL that accepts highly substituted cinnamic acids is available for further studies on branches of phenylpropanoid metabolism that probably lead to the precursors of lignin. Surprisingly the activity levels of the four isoenzymes and steady-state levels of their transcripts were differently affected after elicitor treatment of soybean cell cultures with a b-glucan elicitor of Phytophthora sojae revealing the down-regulation of 4CL1 vs. up-regulation of 4CL3 4. A similar regulation of the transcript levels of the different 4CL isoforms was observed in soybean .

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