Molecular cloning and characterization of phenylalanine ammonia-lyase and cinnamate 4-hydroxylase in the phenylpropanoid biosynthesis pathway in garlic (Allium sativum)

J Agric Food Chem. 2010 Oct 27;58(20):10911-7. doi: 10.1021/jf1021384. Epub 2010 Sep 23.

Abstract

The cDNAs encoding phenylalanine ammonia-lyase (PAL) and cinnamate 4-hydroxylase (C4H) were cloned from garlic (Allium sativum) using reverse transcription-polymerase chain reaction (RT-PCR) with degenerate primers and 5' and 3' rapid amplification of cDNA ends (RACE) PCR. Amino acid sequence alignments showed that AsPAL and AsC4H have more than 70% amino acid identity with their homologues in other plants. The expression of AsPAL and AsC4H transcripts was highest in the roots but surprisingly low in the bulbils, where phenylpropanoid compounds are most concentrated. These results suggest that some phenylpropanoids are synthesized in the roots and subsequently transported to the bulbils of A. sativum .

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Cloning, Molecular*
  • Garlic / chemistry
  • Garlic / classification
  • Garlic / enzymology*
  • Garlic / genetics
  • Gene Expression Regulation, Plant
  • Molecular Sequence Data
  • Phenylalanine Ammonia-Lyase / chemistry
  • Phenylalanine Ammonia-Lyase / genetics*
  • Phenylalanine Ammonia-Lyase / metabolism
  • Phylogeny
  • Plant Proteins / chemistry
  • Plant Proteins / genetics*
  • Plant Proteins / metabolism
  • Sequence Alignment
  • Trans-Cinnamate 4-Monooxygenase / chemistry
  • Trans-Cinnamate 4-Monooxygenase / genetics*
  • Trans-Cinnamate 4-Monooxygenase / metabolism

Substances

  • Plant Proteins
  • Trans-Cinnamate 4-Monooxygenase
  • Phenylalanine Ammonia-Lyase