Isolation and molecular characterization of cinnamate 4-hydroxylase from apricot and plum

A. Pina, Tetyana Zhebentyayeva, P. Errea, A. Abbott

Research output: Contribution to journalArticle

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Abstract

Cinnamate 4-hydroxylase (C4H) is the second enzyme in the phenylpropanoid pathway which participates in the synthesis of numerous phenylpropanoid compounds such as flavonoids, lignins, suberins and others. We identified a gene putatively coding for Class I C4H in apricot and plum and we analyzed the expression pattern of this gene under different apricot/plum graft combinations with different degree of compatibility. The full-length cDNA is 1 739 bp with a 1 515 bp open reading frame encoding a protein of 504 amino acids. Like other C4Hs, the predicted C4H polypeptides included conserved domains of cytochrome P 450. The genomic sequence of the apricot C4H gene was interrupted by two introns 335 bp and 904 bp long. Several regulatory motifs including P-, A-, L- and H-boxes, which were conserved across phenylpropanoid metabolism-related genes in higher plants, were found in a 1 300 bp upstream promoter region of the apricot C4H gene. A phylogenetic analysis showed that all Prunus sequences clustered together and were closely related to Malus and Rubus C4H genes. The transcription of Class I PruC4H was detected in all the examined graft combinations, which suggested its rather constitutive character.

Original languageEnglish (US)
Pages (from-to)441-450
Number of pages10
JournalBiologia Plantarum
Volume56
Issue number3
DOIs
Publication statusPublished - Sep 1 2012

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All Science Journal Classification (ASJC) codes

  • Plant Science
  • Horticulture

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