Skip to main content
Data in Brief logoLink to Data in Brief
. 2022 Feb 2;41:107890. doi: 10.1016/j.dib.2022.107890

Label-free proteome data of susceptible and resistant rice cultivars in response to Xanthomonas oryzae pv. oryzae inoculation

Ravi Gupta a, Cheol Woo Min b, Sang-Ryeol Park c,, Sun Tae Kim b,
PMCID: PMC8842008  PMID: 35198671

Abstract

Here we report the data associated with the article: “Comparative proteome profiling of susceptible and resistant rice cultivars identified an arginase involved in rice defense against Xanthomonas oryzae pv. oryzae[1]. Bacterial blight disease caused by Xanthomonas oryzae pv. oryzae (Xoo) is one of the most devastating diseases of rice across the globe; however, the underlying molecular mechanism of rice-Xoo interaction is currently not well understood. In this manuscript, we report the proteome profiles of rice leaves generated using a label-free quantitative proteomic analysis using QExactive™ Orbitrap High-Resolution Mass Spectrometer, MapMan, and rice interactome viewer [1].

Keywords: Bacterial blight disease, Plant-pathogen interaction, Plant defense, Signaling, Quantitative proteomics

Specifications Table

Subject Biology
Specific subject area Plant science, Proteomics, Plant-pathogen interaction
Type of data Table, Figure
How the data were acquired QExactive™ Orbitrap High-Resolution Mass Spectrometer (Thermo Fisher Scientific, USA) coupled with UHPLC Dionex UltiMate ® 3000 (Thermo Fisher Scientific, USA) system
Data format Raw, Analyzed
Description of data collection Leaf proteomes of Xoo susceptible (Dongjin) and resistant (Hwayeong) cultivars were analyzed after 0, 3d, and 6d in response to inoculation of K1 strain of Xoo
Data source location Plant Immunity Laboratory, Department of Plant Science, Pusan National University, Miryang, South Korea (latitude 35 N)
Data accessibility With this article. All raw data are deposited in the ProteomeXchange with the dataset identifier PXD027569.
Direct FTP link to data: http://proteomecentral.proteomexchange.org/cgi/GetDataset?ID=PXD027569
Related research article R. Gupta, C.W. Min, S. Son, G.H. Lee, J.W. Jang, S.W. Kwon, S.R. Park, S.T. Kim, Comparative proteome profiling of susceptible and resistant rice cultivars identified an arginase involved in rice defense against Xanthomonas oryzae pv. oryzae, Plant Physio. Biochem. 171 (2022) 105–114 [1].

Value of the Data

  • Data reported here show the comparative protein profiles of two rice cultivars that are susceptible (Dongjin) and resistant (Hwayeong) to Xoo strain KACC10859 (K1).

  • This data show that the proteins related to photosynthesis and photorespiration were majorly decreased in resistant cultivar while proteins associated with jasmonic acid biosynthesis, protein modification, and proteolysis were majorly increased.

  • Researchers working in the area of plant-pathogen interaction can use this dataset to check the abundance pattern of 4214 identified rice proteins in response to Xoo inoculation.

  • Further, the information derived from this dataset can be translated to other pathosystems to predict the abundance of various host plant proteins in response to pathogen attack.

  • Taken together, this data provide a list of potential protein candidates that can be targeted in the future to generate the Xoo resistant rice cultivars.

1. Data Description

The dataset reported here was obtained from the proteome analysis of two rice cultivars Dongjin and Hwayeong challenged with the K1 strain of Xoo. A shotgun proteomics approach was utilized for the identification of proteins and a label-free approach was utilized for their quantification. Downstream data processing and filtering were performed using Perseus software (Fig. 1) and functional annotation of the Xoo responsive proteins in the two cultivars was carried out by MapMan analysis (Figs. 2,3 and 5). Interactions among the Hwayeong specific proteins were analyzed by rice interactome viewer (Fig. 4). Supplementary Tables 1, 2, and 3, representatively show the list of Xoo responsive rice proteins (Supplementary Table. 1), Hwayeong and Dongjin specific proteins (Supplementary Table. 2), and results of interactome analysis (Supplementary Table. 3).

Fig. 1.

Fig 1

Multi-scatterplots showing pearson correlation coefficient values among different replicates of the samples.

Fig. 2.

Fig 2

Major CHO metabolism overview category of MapMan showing differential modulation of Dongjin and Hwayeong proteins corresponding to clusters 1 and 2 of Fig. 2A.

Fig. 3.

Fig 3

Regulation overview category of MapMan showing differential modulation of Dongjin and Hwayeong proteins corresponding to clusters 1 and 2 of Fig. 2A.

Fig. 5.

Fig 5

Jasmonic acid biosynthesis pathway showing significantly modulated proteins marked by red (increased abundance) and green (decreased abundance) color scheme.

Fig. 4.

Fig 4

Interaction network showing experimentally confirmed interactions among the Hwayeong specific proteins.

2. Experimental Design, Materials and Methods

2.1. Plant materials

Oryzae sativa ssp. japonica cultivars Dongjin and Hwayeong seeds were surface-sterilized sequentially with 70% ethanol for 1 min and 5% sodium hypochlorite for 5 min. These seeds were then planted in the soil after their complete washing in deionized water and allowed to germinate and at 28 °C with a 16 h/8 h day/night cycle.

2.2. Xoo treatment and protein extraction

Xoo strain KACC10859 (K1) showing compatible and incompatible interactions with Dongjin and Hwayeong rice cultivars was used for the experimentation. Xoo was cultured in PSA agar media and was inoculated on rice leaves using a clipping method as described previously [2]. Extraction of rice leaf proteins and enrichment of low-abundance proteins were carried out as described in detail previously [3]. In brief, 1 g of Dongjin and Hwayeong leaves harvested after 0,3 and 6 days were powdered using liquid nitrogen followed by the addition of 10 mL of Tris-Mg/NP-40 buffer and centrifugation at 12,000 × g for 15 min at 4 °C. The supernatant obtained after centrifuge was treated with 0.1% Protamine Sulfate (w/v, in deionized water) for 30 min to enrich the low-abundance proteins which were subsequently used for the proteome analysis.

2.3. Label-free quantitative proteome analysis with Q-Exactive

The isolated proteins were carried out label-free quantitative proteome analysis using QExactive ™ Orbitrap High-Resolution Mass Spectrometer (Thermo Fisher Scientific, USA) coupled with UHPLC Dionex UltiMate ® 3000 (Thermo Fisher Scientific, USA) system as described previously [1]. In brief, rice leaf proteins were digested using in-solution trypsin digestion and further mass spectrometry analysis was carried out as described in detail previously [1] (Supplementary Tables. 1 and 2). The mass spectrometry proteomics data have been deposited to the ProteomeXchange Consortium via the PRIDE [4] partner repository with the dataset identifier PXD027569 and can be accessed at https://www.ebi.ac.uk/pride/archive/projects/PXD027569.

2.5. Statistical test and functional classification

Analysis of raw mass spectrometry data and label-free quantitative proteome analysis was carried out using the MaxQuant software with integrated Andromeda search engine [5]. Further downstream data processing and the statistical test were performed using Perseus software [6]. Multiple sample test was performed to find out significant differences (≥1.5 fold change, Benjamini-Hochberg-based FDR < 0.05) in the protein abundance following Xoo treatment (Supplementary Tables. 1 and 2). Differential proteins were functionally annotated using MapMan software [7].

Ethics Statements

No animal experiments were performed in this study.

CRediT authorship contribution statement

Ravi Gupta: Conceptualization, Methodology, Software, Writing – original draft. Cheol Woo Min: . Sang-Ryeol Park: . Sun Tae Kim: Supervision, Writing – review & editing.

Declaration of Competing Interest

The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.

Acknowledgments

This study was carried out with the support of “Research Program for Agricultural Science & Technology Development (Project No. PJ01570601) of National Institute of Agricultural Sciences, Rural Development Administration, Republic of Korea and by National Research Foundation of Korea (NRF) through the leading research supporting program (grant no. 2019R1A2C2085868 and 2021R1A4A2001968 provided to STK).

Footnotes

Supplementary material associated with this article can be found, in the online version, at doi:10.1016/j.dib.2022.107890.

Contributor Information

Sang-Ryeol Park, Email: srpark@korea.kr.

Sun Tae Kim, Email: stkim71@pusan.ac.kr.

Appendix. Supplementary materials

Supplementary Table. 1. List of common and Xoo responsive leaf proteins of Dongjin and Hwayeong cultivars.

mmc1.xlsx (1.4MB, xlsx)

Supplementary Table. 2. List of the Dongjin and Hwayeong specific proteins.

mmc2.xlsx (301.8KB, xlsx)

Supplementary Table. 3. List of Hwayeong proteins showing interactions among other proteins as identified by Rice Interactome Viewer.

mmc3.xlsx (13.8KB, xlsx)

References

  • 1.Gupta R., Min C.W., Son S., Lee G.H., Jang J.W., Kwon S.W., Park S.R., Kim S.T. Comparative proteome profiling of susceptible and resistant rice cultivars identified an arginase involved in rice defense against Xanthomonas oryzae pv. oryzae. Plant Physiol. Biochem. 2022;171:105–114. doi: 10.1016/j.plaphy.2021.12.031. [DOI] [PubMed] [Google Scholar]
  • 2.Wang Y., Gupta R., Song W., Huh H.H., Lee S.E., Wu J., Agrawal G.K., Rakwal R., Kang K.Y., Park S.R., Kim S.T. Label-free quantitative secretome analysis of Xanthomonas oryzae pv. oryzae highlights the involvement of a novel cysteine protease in its pathogenicity. J. Proteom. 2017;169:202–214. doi: 10.1016/j.jprot.2017.02.012. [DOI] [PubMed] [Google Scholar]
  • 3.Gupta R., Kim S.T. Depletion of RuBisCo protein using the protamine sulfate precipitation method. Methods Mol Biol. 2015;1295:225–233. doi: 10.1007/978-1-4939-2550-6_17. [DOI] [PubMed] [Google Scholar]
  • 4.Vizcaíno J.A., Csordas A., Del-Toro N., Dianes J.A., Griss J., Lavidas I., Mayer G., Perez-Riverol Y., Reisinger F., Ternent T., Xu Q.W., Wang R., Hermjakob H. 2016 update of the PRIDE database and its related tools. Nucleic Acids Res. 2016;44:447–456. [Google Scholar]
  • 5.Tyanova S., Temu T., Cox J. The MaxQuant computational platform for mass spectrometry - based shotgun proteomics. Nat. Protoc. 2016;11:2301–2319. doi: 10.1038/nprot.2016.136. [DOI] [PubMed] [Google Scholar]
  • 6.Tyanova S., Temu T., Sinitcyn P., Carlson A., Hein M.Y., Geiger T., Mann M., Cox J. The perseus computational platform for comprehensive analysis of (prote) omics data. Nat. Methods. 2016;13:731–740. doi: 10.1038/nmeth.3901. [DOI] [PubMed] [Google Scholar]
  • 7.Thimm O., Bläsing O., Gibon Y., Nagel A., Meyer S., Krüger P., Selbig J., Müller L.A., Rhee S.Y., Stitt M. mapman: a user-driven tool to display genomics data sets onto diagrams of metabolic pathways and other biological processes. Plant J. 2004;37:914–939. doi: 10.1111/j.1365-313x.2004.02016.x. [DOI] [PubMed] [Google Scholar]

Associated Data

This section collects any data citations, data availability statements, or supplementary materials included in this article.

Supplementary Materials

Supplementary Table. 1. List of common and Xoo responsive leaf proteins of Dongjin and Hwayeong cultivars.

mmc1.xlsx (1.4MB, xlsx)

Supplementary Table. 2. List of the Dongjin and Hwayeong specific proteins.

mmc2.xlsx (301.8KB, xlsx)

Supplementary Table. 3. List of Hwayeong proteins showing interactions among other proteins as identified by Rice Interactome Viewer.

mmc3.xlsx (13.8KB, xlsx)

Articles from Data in Brief are provided here courtesy of Elsevier

RESOURCES