PXD010457-1

PXD010457 is an original dataset announced via ProteomeXchange.

Title	Proteomic profiling of peroxisomal proteins in the ripening of sweet pepper (Capsicum annuum L.) fruit. Catalase as a case study
Description	Fruit ripening is a very important physiological process which gains relevance in crop species due to their economical and nutritional repercussions. During fruit ripening enormous metabolic changes occur in a genetically-controlled scenario affecting the physiology of most cell compartments. Peroxisomes are single-membrane bounded organelles present in all eukaryotes which display a noteworthy nitro-oxidative metabolism, and harbor catalase as one of the major antioxidant enzymes in cells. Quantitative proteomics analysis by isobaric tags for relative and absolute quantification (iTRAQ) was used to investigate the ripening process in sweet pepper (Capsicum annuum L.) fruits. Out of 2,574 quantified proteins, 692 were found to be significantly more abundant in immature green fruits compared to red ones, but 497 showed a lower expression as the ripening proceeded. Overall, about 50% of the detectable proteins were estimated to modify their expression due to the ripening process. Data obtained from the Gene Ontology algorithms (AgriGO platform) showed that from all the identified proteins, 46 (2%) were only predicted to have a peroxisomal origin, with a high number of them displaying up-expression tendency during ripening. Catalase was framed within the group which showed lower expression in ripe fruits, but this enzyme was also susceptible to undergo posttranslational modifications (PTMs) promoted by reactive nitrogen and oxygen species (RNS and ROS) through nitration, S-nitrosylation and oxidation events which provoked its inhibition. The biochemical characterization of catalase indicates that it has atypical native molecular mass (125-135 kDa), since it behaves as a homodimer, and isoelectric point of 7.4, which is higher than that of the majority of plant catalases reported so far. Taking together, these data suggest that ROS and RNS could be essential to modulate the role of catalase for the maintenance of basic cellular peroxisomal functions during pepper fruit ripening where nitro-oxidative stress occur.
HostingRepository	PRIDE
AnnounceDate	2022-05-19
AnnouncementXML	Submission_2022-05-19_02:16:27.849.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Antonio Ramos Fernández
SpeciesList	scientific name: Capsicum annuum; NCBI TaxID: 4072;
ModificationList	2-pyrrolidone-5-carboxylic acid (Glu); 2-pyrrolidone-5-carboxylic acid (Gln); iTRAQ8plex-116 reporter+balance reagent acylated residue; monohydroxylated residue; acetylated residue; iodoacetamide derivatized residue
Instrument	TripleTOF 5600

Revision	Datetime	Status	ChangeLog Entry
0	2018-07-17 05:28:53	ID requested
⏵ 1	2022-05-19 02:16:28	announced
2	2024-10-22 05:36:18	announced	2024-10-22: Updated project metadata.

Gonz, á, lez-Gordo S, Rodr, í, guez-Ruiz M, L, ó, pez-Jaramillo J, Mu, ñ, oz-Vargas MA, Palma JM, Corpas FJ, L.) Fruits. Antioxidants (Basel), 11(4):(2022) [pubmed]

curator keyword: Biological

submitter keyword: catalase, iTRAQ, molecular characterization, pepper fruits ripening, peroxisomes, protein expression, reactive oxygen especies, reactive nitrogen species.

José Manuel Palma Martínez
contact affiliation	Estación Experimental del Zaidín, CSIC, Granada, Spain
contact email	josemanuel.palma@eez.csic.es
lab head
Antonio Ramos Fernández
contact affiliation	Proteobotics S.L.
contact email	aramos@proteobotics.com
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD010457
     1. Label: PRIDE project
     2. Name: Proteomic profiling of peroxisomal proteins in the ripening of sweet pepper (Capsicum annuum L.) fruit. Catalase as a case study