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Characterization and expression profiling of cinnamate 4-hydroxylase gene from Salvia miltiorrhiza in rosmarinic acid biosynthesis pathway

Characterization and expression profiling of cinnamate 4-hydroxylase gene from Salvia... A novel cinnamate 4-hydroxylase (C4H) gene (designated as SmC4H) involved in the rosmarinic acid biosynthesis pathway is cloned from Salvia miltiorrhiza. The full-length cDNA of SmC4H is 1800 bp long with an open reading frame of 1512 bp encoding a polypeptide of 504 amino acid residues. Like other C4Hs, the predicted SmC4H polypeptide includes three domains: a heme-binding domain, a proline-rich region, and a P450 (E)EFRPER-motif region, which represents a typical structure of plant C4Hs. Analysis of SmC4H genomic DNA reveals that it contains 3 exons, 2 introns, the length of exons being highly conserved. Semiquantitative RT-PCR analysis revealed that the constitutive expression of SmC4H in the root or stem was much higher than in the leaf. Further expression analysis revealed that the signaling components of defense/stress pathways, such as methyl jasmonate, abscisic acid, and ultraviolet-B radiation, up-regulated the SmC4H transcript levels over the control. Calcium chloride and hydrogen peroxide, nevertheless, had no significant effect on SmC4H expression. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Russian Journal of Plant Physiology Springer Journals

Characterization and expression profiling of cinnamate 4-hydroxylase gene from Salvia miltiorrhiza in rosmarinic acid biosynthesis pathway

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Publisher
Springer Journals
Copyright
Copyright © 2008 by MAIK Nauka
Subject
Life Sciences; Plant Sciences ; Plant Physiology
ISSN
1021-4437
eISSN
1608-3407
DOI
10.1134/S1021443708030163
Publisher site
See Article on Publisher Site

Abstract

A novel cinnamate 4-hydroxylase (C4H) gene (designated as SmC4H) involved in the rosmarinic acid biosynthesis pathway is cloned from Salvia miltiorrhiza. The full-length cDNA of SmC4H is 1800 bp long with an open reading frame of 1512 bp encoding a polypeptide of 504 amino acid residues. Like other C4Hs, the predicted SmC4H polypeptide includes three domains: a heme-binding domain, a proline-rich region, and a P450 (E)EFRPER-motif region, which represents a typical structure of plant C4Hs. Analysis of SmC4H genomic DNA reveals that it contains 3 exons, 2 introns, the length of exons being highly conserved. Semiquantitative RT-PCR analysis revealed that the constitutive expression of SmC4H in the root or stem was much higher than in the leaf. Further expression analysis revealed that the signaling components of defense/stress pathways, such as methyl jasmonate, abscisic acid, and ultraviolet-B radiation, up-regulated the SmC4H transcript levels over the control. Calcium chloride and hydrogen peroxide, nevertheless, had no significant effect on SmC4H expression.

Journal

Russian Journal of Plant PhysiologySpringer Journals

Published: May 15, 2008

References