Summary of Study ST002430

This data is available at the NIH Common Fund's National Metabolomics Data Repository (NMDR) website, the Metabolomics Workbench, https://www.metabolomicsworkbench.org, where it has been assigned Project ID PR001563. The data can be accessed directly via it's Project DOI: 10.21228/M8NX4M This work is supported by NIH grant, U2C- DK119886.

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This study contains a large results data set and is not available in the mwTab file. It is only available for download via FTP as data file(s) here.

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Study IDST002430
Study TitleInsights from a Multi-Omics Integration (MOI) Study in Oil Palm (Elaeis guineensis Jacq.) Response to Abiotic Stresses: Part Two—Drought
Study TypeMulti-Omics Integration (MOI) Study
Study SummaryDrought and salinity are two of the most severe abiotic stresses affecting agriculture Worldwide and bear some similarities in the response of plants to them. The first is also known as osmotic stress and shows similarities mainly with the osmotic effect, the first phase of salinity stress. Multi-Omics Integration (MOI) offers a new opportunity for the non-trivial challenge of unraveling the mechanisms behind multigenic traits, such as drought and salinity resistance. The current study carried out a comprehensive, large-scale, single-omics analysis (SOA) and MOI studies on the leaves of young oil palm plants submitted to water deprivation. After performing SOA, 1,955 DE enzymes from transcriptomics analysis, 131 DE enzymes from proteomics analysis, and 269 DE metabolites underwent MOI analysis, revealing several pathways affected by this stress, with at least one DE molecule in all three omics platforms used. Besides, the similarities and dissimilarities in the molecular response of those plants to those two abiotic stresses underwent mapping. Cysteine and methionine metabolism (map00270) was the most affected pathway in all scenarios evaluated. The correlation analysis revealed that 91.55% of those enzymes expressed under both stresses had similar qualitative profiles, corroborating the already known fact that plant responses to drought and salinity show several similarities. At last, the results shed light on some candidate genes for engineering crop species resilient to both abiotic stresses.
Institute
The Brazilian Agricultural Research Corporation (Embrapa)
DepartmentEmbrapa Agroenergy
LaboratoryGenetics and Plant Biotechnology
Last NameSouza Jr
First NameManoel Teixeira
AddressParque Estacao Biologica, Final Avenida W3 Norte - Asa Norte, Brasilia, Distrito Federal, 70770901, Brazil
Emailmanoel.souza@embrapa.br
Phone+55.61.3448.3210
Submit Date2022-09-28
Publicationshttps://doi.org/10.1038/s41598-021-97835-x
Raw Data AvailableYes
Raw Data File Type(s)mzXML
Analysis Type DetailLC-MS
Release Date2023-01-20
Release Version1
Manoel Teixeira Souza Jr Manoel Teixeira Souza Jr
https://dx.doi.org/10.21228/M8NX4M
ftp://www.metabolomicsworkbench.org/Studies/ application/zip

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Sample Preparation:

Sampleprep ID:SP002525
Sampleprep Summary:Leaf samples with approximately 50 mg were collected for the metabolomics analysis; four replicates per plant. After harvesting, samples were immediately frozen in liquid nitrogen and stored at − 80 °C until metabolites extraction and analysis. Each sample was ground in a ball mill (Biospec Products, USA) before solvent extraction. Metabolites were extracted using an adapted protocol from The Max Planck Institute, called All-in-One, which provides a polar fraction for secondary metabolite analysis, a nonpolar fraction for lipidomics, and a protein pellet for proteomics; all obtained from the same plant sample. Each ground sample was added to a microtube and mixed with 1 mL of a methanol and methyl-tert-butyl-ether (1:3) solution at − 20°C. After homogenization, they were incubated at 4 °C for 10 min. Each microtube was ultrasonicated in an ice bath for another 10 min. Then, 500 μL of a methanol and water (1:3) solution was added to the microtube before centrifugation (12,000 rpm at 4 °C for 5 min). Three phases were separate: an upper non-polar (green), a lower polar (brown), and a remaining protein pellet. Samples were transferred to fresh microtubes and vacuum-dried in a speed vac (Centrivap, Labconco, Kansas City, MO, USA) overnight at room temperature (~ 22 °C).
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