Gene structure of PACO1, a petal senescence‐related related gene from Phalaenopsis encoding peroxisomal acyl‐CoA oxidase homolog

Do, Yi‐Yin; Huang, Pung‐Ling

doi:10.1080/15216549700201641

Cited by 4 publications

(1 citation statement)

References 9 publications

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“…It appeared to be a single copy gene whose expression is induced by exogenous application of ethylene. A genomic clone of PACO1 was isolated from a genomic DNA library of Phalaenopsis with the intention to analyze the promoter sequence and further characterize the activity of this gene in orchids (Do and Huang, 1997).…”

Section: Featurementioning

confidence: 99%

Orchid Biotechnology in Production and Improvement

Mudalige¹,

Kuehnle²

2004

HortSci

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Section: Featurementioning

confidence: 99%

Orchid Biotechnology in Production and Improvement

Mudalige¹,

Kuehnle²

2004

HortSci

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Agarwal

Bhat

et al. 2001

Plant Molecular Biology

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The first committed step in the beta-oxidation of fatty acids is catalyzed by the enzyme acyl-CoA oxidase (ACOX), which oxidizes a fatty acyl-CoA to a 2-trans-enoyl-CoA. To understand the role of beta-oxidation during seedling growth in soybean, two ACOX cDNAs were isolated by screening a seedling library with a DNA fragment obtained by RT-PCR by using degenerate oligonucleotides. The two cDNAs (ACX1;1 and ACX1;2) are 86% identical to each other at the nucleotide and the amino acid level. Their deduced amino acid sequences share significant homology with known acyl-CoA oxidases, including the conserved CGGHGY motif, a putative flavin mononucleotide binding site. In both sequences, the last three amino acids, ARL, represent a putative peroxisome targeting signal. The mRNA and protein of both cDNAs accumulated in all seedling tissues, with relatively stronger expression in the growing seedling axis and hypocotyl, and weaker expression in the cotyledon. Immunolocalization studies indicated that the two proteins were localized in the phloem cells of hypocotyl tissue. The two cDNAs were expressed in Escherichia coli and shown to possess acyl-CoA oxidase activity. With fatty acyl-CoA substrates of varying chain lengths, it was demonstrated that both ACX1;1 and ACX1;2 have broad substrate specificities (C8-C18). The stronger expression of ACX1;1 and ACX 1;2 in the axis and hypocotyl tissue, the weaker expression in the oil-rich cotyledon tissue, and the broad substrate specificities suggest that the two acyl-CoA oxidases might play a general house-keeping role during soybean seedling growth, such as the turnover of membrane lipids.

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Untitled

Rubinstein

2000

Plant Molecular Biology

142

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The often rapid and synchronous programmed death of petal cells provides a model system to study molecular aspects of organ senescence. The death of petal cells is preceded by a loss of membrane permeability, due in part to increases in reactive oxygen species that are in turn related to up-regulation of oxidative enzymes and to a decrease in activity of certain protective enzymes. The senescence process also consists of a loss of proteins caused by activation of various proteinases, a loss of nucleic acids as nucleases are activated, and enzyme-mediated alterations of carbohydrate polymers. Many of the genes for these senescence-associated enzymes have been cloned. In some flowers, the degradative changes of petal cells are initiated by ethylene; in others, abscisic acid may play a role. External factors such as pollination, drought and temperature stress also affect senescence, perhaps by interacting with hormones normally produced by the flowers. Signal transduction may involve G-proteins, calcium activity changes and the regulation of protein phosphorylation and dephosphorylation. The efficacy of the floral system as well as the research tools now available make it likely that important information will soon be added to our knowledge of the molecular mechanisms involved in petal cell death.

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Gene structure of PACO1, a petal senescence‐related related gene from Phalaenopsis encoding peroxisomal acyl‐CoA oxidase homolog

Cited by 4 publications

References 9 publications

Orchid Biotechnology in Production and Improvement

Orchid Biotechnology in Production and Improvement

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