Molecular cloning and characterization of phenylalanine ammonia-lyase and cinnamate 4-hydroxylase in the phenylpropanoid biosynthesis pathway in garlic (Allium sativum).
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 .
Tuan
Pham Anh
PA
Department of Crop Science, College of Agriculture and Life Sciences, Chungnam National University, 220 Gung-Dong, Yuseong-Gu, Daejeon 305-764, Korea.
Park
Nam Il
NI
Li
Xiaohua
X
Xu
Hui
H
Kim
Haeng Hoon
HH
Park
Sang Un
SU
D000595:Amino Acid Sequence; D003001:Cloning, Molecular; D005737:Garlic / Q000737:chemistry / Q000145:classification / Q000201:enzymology* / Q000235:genetics; D018506:Gene Expression Regulation, Plant; D008969:Molecular Sequence Data; D010650:Phenylalanine Ammonia-Lyase / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D010802:Phylogeny; D010940:Plant Proteins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D016415:Sequence Alignment; D050564:Trans-Cinnamate 4-Monooxygenase / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism
D010940:Plant Proteins; D050564:Trans-Cinnamate 4-Monooxygenase; D010650:Phenylalanine Ammonia-Lyase