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: Article

4 Citas (Scopus)

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.

Idioma originalEnglish
Páginas (desde-hasta)46-54
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

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.
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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.",
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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: Article

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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