ArticleMolecular biology reports2013
Cloning, identification and expression analysis of ACC oxidase gene involved in ethylene production pathway.
Article in Molecular biology reports, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 22 citations in OpenAlex.
- Ethylene biosynthesis in legumes: gene identification and expression during early symbiotic stages.Journal of experimental botany · 2025Article
- The triggering mechanism for predominant hormonal signal production in fleshy fruit ripening.Molecular horticulture · 2025Review
- Both TwoFrontiers in plant science · 2022Article
- Roots drive oligogalacturonide-induced systemic immunity in tomato.Plant, cell & environment · 2021Article
- 1-Aminocyclopropane-1-Carboxylic Acid Oxidase (ACO): The Enzyme That Makes the Plant Hormone Ethylene.Frontiers in plant science · 2019Review
- Transcriptome Analysis of Cell Wall and NAC Domain Transcription Factor Genes duringFrontiers in plant science · 2017Article
- Comprehensive RNA-Seq Analysis on the Regulation of Tomato Ripening by Exogenous Auxin.PloS one · 2016Article
- Genome-Wide Transcriptional Profiling and Metabolic Analysis Uncover Multiple Molecular Responses of the Grass Species Lolium perenne Under Low-Intensity Xenobiotic Stress.Frontiers in plant science · 2015Article
- Ethylene, a Hormone at the Center-Stage of Nodulation.Frontiers in plant science · 2015Review
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
1-aminocyclopropane-1-carboxylic acid oxidase (ACO) enzyme is a member of the Fe II-dependent family of oxidases/oxygenases which require Fe(2+) as a cofactor, ascorbate as a cosubstrate and CO(2) as an activator. This enzyme catalyses the terminal step in the plant signaling of ethylene biosynthetic pathway. A 948 bp fragment of the ACO1 gene cDNA sequence was cloned from tomato (Lycopersicon esculentum) fruit tissues by using reverse transcriptase-polymerase chain reaction (RT-PCR) with two PCR primers designed according to the sequence of a tomato cDNA clone (X58273). The BLAST search showed a high level of similarity (77-98 %) between ACO1 and ACO genes of other plants. The calculated molecular mass and predicted isoelectric point of LeACO1 were 35.8 kDa and 5.13, respectively. The three-dimensional structure studies illustrated that the LeACO1 protein folds into a compact jelly-roll motif comprised of 8 α-helices, 12 β-strands and several long loops. The cosubstrate was located in a cofactor-binding pocket referred to as a 2-His-1-carboxylate facial triad. Semi-quantitative RT-PCR analysis of gene expression revealed that the LeACO1 was expressed in fruit tissues at different ripening stages.
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