A catechol oxidase AcPPO from cherimoya (Annona cherimola Mill.) is localized to the Golgi apparatus

Patricio Olmedo, Adrián A. Moreno, Dayan Sanhueza, Iván Balic, Christian Silva-Sanzana, Baltasar Zepeda, Julian C. Verdonk, César Arriagada, Claudio Meneses, Reinaldo Campos-Vargas

Resultado de la investigación: Contribución a la publicaciónArticle

  • 2 Citas

Resumen

Cherimoya (Annona cherimola) is an exotic fruit with attractive organoleptic characteristics. However, it is highly perishable and susceptible to postharvest browning. In fresh fruit, browning is primarily caused by the polyphenol oxidase (PPO) enzyme catalyzing the oxidation of o-diphenols to quinones, which polymerize to form brown melanin pigment. There is no consensus in the literature regarding a specific role of PPO, and its subcellular localization in different plant species is mainly described within plastids. The present work determined the subcellular localization of a PPO protein from cherimoya (AcPPO). The obtained results revealed that the AcPPO- green fluorescent protein co-localized with a Golgi apparatus marker, and AcPPO activity was present in Golgi apparatus-enriched fractions. Likewise, transient expression assays revealed that AcPPO remained active in Golgi apparatus-enriched fractions obtained from tobacco leaves. These results suggest a putative function of AcPPO in the Golgi apparatus of cherimoya, providing new perspectives on PPO functionality in the secretory pathway, its effects on cherimoya physiology, and the evolution of this enzyme.

IdiomaEnglish
Páginas46-54
Número de páginas9
PublicaciónPlant Science
Volumen266
DOI
EstadoPublished - 1 ene 2018

Huella dactilar

Annona
Annona cherimola
Catechol Oxidase
Golgi Apparatus
Golgi apparatus
catechol oxidase
Fruit
introduced plants
melanin
raw fruit
enzymes
Quinones
quinones
green fluorescent protein
Plastids
Secretory Pathway
plastids
Melanins
Enzymes
Green Fluorescent Proteins

Keywords

    ASJC Scopus subject areas

    • Genetics
    • Agronomy and Crop Science
    • Plant Science

    Citar esto

    Olmedo, Patricio ; Moreno, Adrián A. ; Sanhueza, Dayan ; Balic, Iván ; Silva-Sanzana, Christian ; Zepeda, Baltasar ; Verdonk, Julian C. ; Arriagada, César ; Meneses, Claudio ; Campos-Vargas, Reinaldo. / A catechol oxidase AcPPO from cherimoya (Annona cherimola Mill.) is localized to the Golgi apparatus. En: Plant Science. 2018 ; Vol. 266. pp. 46-54
    @article{747502e71d5444c78f93e3c19f526012,
    title = "A catechol oxidase AcPPO from cherimoya (Annona cherimola Mill.) is localized to the Golgi apparatus",
    abstract = "Cherimoya (Annona cherimola) is an exotic fruit with attractive organoleptic characteristics. However, it is highly perishable and susceptible to postharvest browning. In fresh fruit, browning is primarily caused by the polyphenol oxidase (PPO) enzyme catalyzing the oxidation of o-diphenols to quinones, which polymerize to form brown melanin pigment. There is no consensus in the literature regarding a specific role of PPO, and its subcellular localization in different plant species is mainly described within plastids. The present work determined the subcellular localization of a PPO protein from cherimoya (AcPPO). The obtained results revealed that the AcPPO- green fluorescent protein co-localized with a Golgi apparatus marker, and AcPPO activity was present in Golgi apparatus-enriched fractions. Likewise, transient expression assays revealed that AcPPO remained active in Golgi apparatus-enriched fractions obtained from tobacco leaves. These results suggest a putative function of AcPPO in the Golgi apparatus of cherimoya, providing new perspectives on PPO functionality in the secretory pathway, its effects on cherimoya physiology, and the evolution of this enzyme.",
    keywords = "Annonaceae, Polyphenol oxidase, Secretory pathway",
    author = "Patricio Olmedo and Moreno, {Adri{\'a}n A.} and Dayan Sanhueza and Iv{\'a}n Balic and Christian Silva-Sanzana and Baltasar Zepeda and Verdonk, {Julian C.} and C{\'e}sar Arriagada and Claudio Meneses and Reinaldo Campos-Vargas",
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    pages = "46--54",
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    Olmedo, P, Moreno, AA, Sanhueza, D, Balic, I, Silva-Sanzana, C, Zepeda, B, Verdonk, JC, Arriagada, C, Meneses, C & Campos-Vargas, R 2018, 'A catechol oxidase AcPPO from cherimoya (Annona cherimola Mill.) is localized to the Golgi apparatus' Plant Science, vol. 266, pp. 46-54. DOI: 10.1016/j.plantsci.2017.10.012

    A catechol oxidase AcPPO from cherimoya (Annona cherimola Mill.) is localized to the Golgi apparatus. / Olmedo, Patricio; Moreno, Adrián A.; Sanhueza, Dayan; Balic, Iván; Silva-Sanzana, Christian; Zepeda, Baltasar; Verdonk, Julian C.; Arriagada, César; Meneses, Claudio; Campos-Vargas, Reinaldo.

    En: Plant Science, Vol. 266, 01.01.2018, p. 46-54.

    Resultado de la investigación: Contribución a la publicaciónArticle

    TY - JOUR

    T1 - A catechol oxidase AcPPO from cherimoya (Annona cherimola Mill.) is localized to the Golgi apparatus

    AU - Olmedo,Patricio

    AU - Moreno,Adrián A.

    AU - Sanhueza,Dayan

    AU - Balic,Iván

    AU - Silva-Sanzana,Christian

    AU - Zepeda,Baltasar

    AU - Verdonk,Julian C.

    AU - Arriagada,César

    AU - Meneses,Claudio

    AU - Campos-Vargas,Reinaldo

    PY - 2018/1/1

    Y1 - 2018/1/1

    N2 - Cherimoya (Annona cherimola) is an exotic fruit with attractive organoleptic characteristics. However, it is highly perishable and susceptible to postharvest browning. In fresh fruit, browning is primarily caused by the polyphenol oxidase (PPO) enzyme catalyzing the oxidation of o-diphenols to quinones, which polymerize to form brown melanin pigment. There is no consensus in the literature regarding a specific role of PPO, and its subcellular localization in different plant species is mainly described within plastids. The present work determined the subcellular localization of a PPO protein from cherimoya (AcPPO). The obtained results revealed that the AcPPO- green fluorescent protein co-localized with a Golgi apparatus marker, and AcPPO activity was present in Golgi apparatus-enriched fractions. Likewise, transient expression assays revealed that AcPPO remained active in Golgi apparatus-enriched fractions obtained from tobacco leaves. These results suggest a putative function of AcPPO in the Golgi apparatus of cherimoya, providing new perspectives on PPO functionality in the secretory pathway, its effects on cherimoya physiology, and the evolution of this enzyme.

    AB - Cherimoya (Annona cherimola) is an exotic fruit with attractive organoleptic characteristics. However, it is highly perishable and susceptible to postharvest browning. In fresh fruit, browning is primarily caused by the polyphenol oxidase (PPO) enzyme catalyzing the oxidation of o-diphenols to quinones, which polymerize to form brown melanin pigment. There is no consensus in the literature regarding a specific role of PPO, and its subcellular localization in different plant species is mainly described within plastids. The present work determined the subcellular localization of a PPO protein from cherimoya (AcPPO). The obtained results revealed that the AcPPO- green fluorescent protein co-localized with a Golgi apparatus marker, and AcPPO activity was present in Golgi apparatus-enriched fractions. Likewise, transient expression assays revealed that AcPPO remained active in Golgi apparatus-enriched fractions obtained from tobacco leaves. These results suggest a putative function of AcPPO in the Golgi apparatus of cherimoya, providing new perspectives on PPO functionality in the secretory pathway, its effects on cherimoya physiology, and the evolution of this enzyme.

    KW - Annonaceae

    KW - Polyphenol oxidase

    KW - Secretory pathway

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    U2 - 10.1016/j.plantsci.2017.10.012

    DO - 10.1016/j.plantsci.2017.10.012

    M3 - Article

    VL - 266

    SP - 46

    EP - 54

    JO - Plant Science

    T2 - Plant Science

    JF - Plant Science

    SN - 0168-9452

    ER -

    Olmedo P, Moreno AA, Sanhueza D, Balic I, Silva-Sanzana C, Zepeda B y otros. A catechol oxidase AcPPO from cherimoya (Annona cherimola Mill.) is localized to the Golgi apparatus. Plant Science. 2018 ene 1;266:46-54. Disponible desde, DOI: 10.1016/j.plantsci.2017.10.012