Tomato polyphenol oxidase B is spatially and temporally regulated during development and in response to ethylene

• Published in: Molecules (Basel, Switzerland) Vol. 16; no. 1; pp. 493 - 517
• Main Authors: Newman, Sally M, Tantasawat, Piyada, Steffens, John C
• Format: Journal Article
• Language: English
• Published: Switzerland MDPI AG 11.01.2011; MDPI
• Subjects: Base Sequence; Biosynthesis; Catechol Oxidase - genetics; Catechol Oxidase - metabolism; Differential expression; Enzymes; ethylene; Ethylenes - pharmacology; Gene Expression Regulation, Enzymologic; Gene Expression Regulation, Plant; Genes; Genetic engineering; Glucuronidase - genetics; GUS; Molecular Sequence Data; Photosynthesis; Plants, Genetically Modified; PPO; promoter analysis; Promoter Regions, Genetic; Proteins; Signal Transduction; Solanum lycopersicum; Solanum lycopersicum - enzymology; Solanum lycopersicum - physiology; transgenic; United States > US
• ISSN: 1420-3049; 1420-3049
• DOI: 10.3390/molecules16010493

Plant polyphenol oxidases (PPOs) are ubiquitous plastid-localized enzymes. A precise analysis of PPO function in plants has been complicated by the presence of several family members with immunological cross reactivity. Previously we reported the isolation of genomic clones coding for the seven members of the tomato (Solanum lycopersicum) PPO family (A, A', B, C, D, E, and F). Here we report the complex spatial and temporal expression of one of the members, PPO B. The PPO B promoter was sequenced and subjected to homology analysis. Sequence similarities were found to nucleotide sequences of genes encoding enzymes/proteins active in the following systems: phenylpropanoid biosynthesis, signal transduction and responsiveness to hormones and stresses, fruit and seed proteins/enzymes, and photosynthesis. Chimeric gene fusions were constructed linking PPO B 5' flanking regions to the reporter gene, b-glucuronidase (GUS). The resultant transgenic plants were histochemically analyzed for GUS activity in various vegetative and reproductive tissues, and evaluated for PPO B responsiveness to ethylene induction. It was shown that PPO B expression was tissue specific, developmentally regulated, ethylene induced, and localized predominantly to mitotic or apoptotic tissues.