Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/276412
Share/Export:
logo share SHARE logo core CORE BASE
Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL | DATACITE

Invite to open peer review
Title

Nitric oxide (NO) differentially modulates the ascorbate peroxidase (APX) isozymes of sweet pepper (Capsicum annuum L.) fruits

AuthorsGonzález-Gordo, Salvador CSIC ORCID; Rodríguez-Ruiz, Marta CSIC ORCID; López-Jaramillo, Javier CSIC ORCID; Muñoz-Vargas, María A. CSIC ORCID; Palma Martínez, José Manuel CSIC ORCID; Corpas, Francisco J. CSIC ORCID
KeywordsAscorbate peroxidase
Fruit ripening
Hydrogen peroxide
Nitric oxide
Nitration
Pepper fruit
Peroxynitrite
S-nitrosation
Ripening
Tyr-nitration
Issue Date2022
PublisherMultidisciplinary Digital Publishing Institute
CitationAntioxidants 11(4): 765 (2022)
AbstractNitric oxide (NO) is a free radical which modulates protein function and gene expression throughout all stages of plant development. Fruit ripening involves a complex scenario where drastic phenotypical and metabolic changes take place. Pepper fruits are one of the most consumed horticultural products worldwide which, at ripening, undergo crucial phenotypical and biochemical events, with NO and antioxidants being implicated. Based on previous transcriptomic (RNA‐Seq), proteomics (iTRAQ), and enzymatic data, this study aimed to identify the ascorbate peroxidase (APX) gene and protein profiles in sweet peppers and to evaluate their potential modulation by NO during fruit ripening. The data show the existence of six CaAPX genes (CaAPX1– CaAPX6) that encode corresponding APX isozymes distributed in cytosol, plastids, mitochondria, and peroxisomes. The time course expression analysis of these genes showed heterogeneous expression patterns throughout the different ripening stages, and also as a consequence of treatment with NO gas. Additionally, six APX isozymes activities (APX I–APX VI) were identified by non‐denaturing PAGE, and they were also differentially modulated during maturation and NO treatment. In vitro analyses of fruit samples in the presence of NO donors, peroxynitrite, and glutathione, showed that CaAPX activity was inhibited, thus suggesting that different posttransla-tional modifications (PTMs), including S‐nitrosation, Tyr‐nitration, and glutathionylation, respec-tively, may occur in APX isozymes. In silico analysis of the protein tertiary structure showed that residues Cys32 and Tyr235 were conserved in the six CaAPXs, and are thus likely potential targets for S‐nitrosation and nitration, respectively. These data highlight the complex mechanisms of the regulation of APX isozymes during the ripening process of sweet pepper fruits and how NO can exert fine control. This information could be useful for postharvest technology; NO regulates H2O2 levels through the different APX isozymes and, consequently, could modulate the shelf life and nutritional quality of pepper fruits.
Publisher version (URL)http://dx.doi.org/10.3390/antiox11040765
URIhttp://hdl.handle.net/10261/276412
DOI10.3390/antiox11040765
Identifiersdoi: 10.3390/antiox11040765
issn: 2076-3921
Appears in Collections:(EEZ) Artículos




Files in This Item:
File Description SizeFormat
2022_Gonzalez_Antioxidants_OA.pdf3,3 MBAdobe PDFThumbnail
View/Open
Show full item record

CORE Recommender

SCOPUSTM   
Citations

23
checked on May 25, 2024

WEB OF SCIENCETM
Citations

16
checked on Feb 26, 2024

Page view(s)

48
checked on May 30, 2024

Download(s)

45
checked on May 30, 2024

Google ScholarTM

Check

Altmetric

Altmetric


This item is licensed under a Creative Commons License Creative Commons