title: Two-dimensional blue native/SDS-PAGE analysis of whole cell lysate protein complexes of rice in response to salt stress.
abstract: To understand the biology of a plant in response to stress, insight into protein-protein interactions, which almost define cell behavior, is thought to be crucial. Here, we provide a comparative complexomics analysis of leaf whole cell lysate of two rice genotypes with contrasting responses to salt using two-dimensional blue native/SDS-PAGE (2D-BN/SDS-PAGE). We aimed to identify changes in subunit composition and stoichiometry of protein complexes elicited by salt. Using mild detergent for protein complex solubilization, we were able to identify 9 protein assemblies as hetero-oligomeric and 30 as homo-oligomeric complexes. A total of 20 proteins were identified as monomers in the 2D-BN/SDS-PAGE gels. In addition to identifying known protein complexes that confirm the technical validity of our analysis, we were also able to discover novel protein-protein interactions. Interestingly, an interaction was detected for glycolytic enzymes enolase (ENO1) and triosephosphate isomerase (TPI) and also for a chlorophyll a-b binding protein and RuBisCo small subunit. To show changes in subunit composition and stoichiometry of protein assemblies during salt stress, the differential abundance of interacting proteins was compared between salt-treated and control plants. A detailed exploration of some of the protein complexes provided novel insight into the function, composition, stoichiometry and dynamics of known and previously uncharacterized protein complexes in response to salt stress.
authors.affiliation: University of Applied Science and Technology, Sari, Mazandaran, Iran.
authors.forename: Amenehsadat
authors.initials: A
authors.lastname: Hashemi
authors.affiliation: Chemical Injuries Research Center, Baqiyatallah University of Medical Sciences, Tehran, Iran. Electronic address: jgharechahi@gmail.com.
authors.forename: Javad
authors.initials: J
authors.lastname: Gharechahi
authors.affiliation: Faculty of Agronomy, University of Agricultural Sciences and Natural Resources of Sari, Sari, Iran.
authors.forename: Ghorbanali
authors.initials: G
authors.lastname: Nematzadeh
authors.affiliation: Department of Molecular Systems Biology at Cell Science Research Center, Royan Institute for Stem Cell Biology and Technology, ACECR, Tehran, Iran.
authors.forename: Faezeh
authors.initials: F
authors.lastname: Shekari
authors.affiliation: Department of Systems Biology, Agricultural Biotechnology Research Institute of Iran, Agricultural Research, Education, and Extension Organization, Karaj, Iran.
authors.forename: Seyed Abdollah
authors.initials: SA
authors.lastname: Hosseini
authors.affiliation: Department of Systems Biology, Agricultural Biotechnology Research Institute of Iran, Agricultural Research, Education, and Extension Organization, Karaj, Iran; Department of Molecular Systems Biology at Cell Science Research Center, Royan Institute for Stem Cell Biology and Technology, ACECR, Tehran, Iran. Electronic address: hsalekdeh@yahoo.com.
authors.forename: Ghasem Hosseini
authors.initials: GH
authors.lastname: Salekdeh
mesh_terms: D002457:Cell Extracts / Q000737:chemistry*; D003902:Detergents / Q000494:pharmacology; D004591:Electrophoresis, Polyacrylamide Gel / Q000379:methods*; D063990:Gene Ontology; D046912:Multiprotein Complexes / Q000378:metabolism; D012275:Oryza / Q000187:drug effects / Q000502:physiology*; D010641:Phenotype; D010940:Plant Proteins / Q000378:metabolism*; D055503:Protein Multimerization / Q000187:drug effects; D054712:Salinity; D012965:Sodium Chloride / Q000494:pharmacology*; D012995:Solubility; D013312:Stress, Physiological / Q000187:drug effects
chemical_list: D002457:Cell Extracts; D003902:Detergents; D046912:Multiprotein Complexes; D010940:Plant Proteins; D012965:Sodium Chloride
keywords: 2D-BN/SDS-PAGE; Complexomics; Protein complexes; Protein-protein interaction; Rice; Salt stress