Proteomic analysis of heat shock proteins in maize (Zea mays L.)

Abstract

Background: Maize is one of the important cereal food crops in the world. High temperature stress causes adverse influence on plant growth. When plants are exposed to high temperatures, they produce heat shock proteins (HSPs), which may impart a generalized role in tolerance to heat stress. Proteome analysis was performed in plant to assess the changes in protein types and their expression levels under abiotic stress. The purpose of the study is to explore which proteins are involved in the response of the maize plant to heat shock treatment. Results:We investigated the responses of abundant proteins of maize leaves, in an Egyptian inbred line of maize "K1", upon heat stress through two-dimensional electrophoresis (2-DE) on samples of maize leaf proteome. 2-DE technique was used to recognize heat-responsive protein spots using Coomassie Brilliant Blue (CBB) and silver staining. In 2-D analysis of proteins from plants treated at 45°C for 2 h, the results manifested 59 protein spots (4.3%) which were reproducibly detected as new spots where did not present in the control. In 2D for treated plants for 4 h, 104 protein spots (7.7%) were expressed only under heat stress. Quantification of spot intensities derived from heat treatment showed that twenty protein spots revealed clear differences between the control and the two heat treatments. Nine spots appeared with more intensity after heat treatments than the control, while four spots appeared only after heat treatments. Five spots were clearly induced after heat treatment either at 2 h or 4 h and were chosen for more analysis by LC-MSMS. They were identified as ATPase beta subunit, HSP26, HSP16.9, and unknown HSP/Chaperonin. Conclusion:The results revealed that the expressive level of the four heat shock proteins that were detected in this study plays important roles to avoid heat stress in maize plants.

Identification and Characterization of Contrasting Genotypes/Cultivars for Developing Heat Tolerance in Agricultural Crops: Current Status and Prospects

“…Proteomics analysis of ethylene pre-treated tomato pollen by LC-MS/MS suggested that various proteins help in protecting pollen development and function through higher abundance of protein synthesis and upregulating stress protecting proteins that maintain cellular redox state under heat stress (Jegadeesan et al, 2018). Proteomics analysis by 2-DE technique allowed identification of important heat shock proteins viz., HSP26, HSP16.9, and unknown HSP/Chaperonin contributing to heat stress tolerance in maize (Abou-Deif et al, 2019). Considering contributory role of proteins adapting roots under heat stress, Valdes-Lopez et al (2016) reported the involvement of both up and down regulatory proteins contributing to heat tolerance in soybean root.…”

Heat Stress Responses and Thermotolerance in Maize

“…In maize, as in Arabidopsis, heat shock activates the expression of both high and low molecular weight HSPs [ 3 , 43 , 44 , 45 , 46 ]. The proteins in maize plants produced in response to heat shock were identified through a proteome analysis and included such proteins as the ATPase beta subunit, HSP26, HSP16.9, and unknown HSP/chaperonin [ 47 , 48 ]. It was actually surprising to find that Hsp26, an early heat stress marker gene, and Hsp17.6 and Hsp18.2 were upregulated under the simulated field conditions when the temperatures were slowly ramped up [ 14 ].…”

Transcriptome Profiling of Elaeis guineensis Jacq. Under Heat Stress Condition

“…The top-five class consisted of a single organism process, biosynthetic process, response to stimulus, oxidation-reduction process, and response stress response. The response stress process sub-category is clustered genes that are regulated under stress [19]. The stimulus-response of an organism is indicated as a process that causes changes in cells activities, secretion, gene expression, enzyme production, and cellular responses.…”

“…Furthermore, HSPs divided into 3 clusters based on their molecular weight consisted of high molecular weight (80-114 kDa), HSP70 (69-71 kDa), and low molecular weight (15-30 kDa). HSPs were consisted of six structurally conserved distinct classes including HSP100, HSP90, HSP70, HSP60 (Chaperonins), small HSPs (sHSPs), and ubiquitin (8,5 kDa) [19]. Major HSPs were synthesized in eukaryotes [20].…”

“…Ubiquitin (8.5 kDa) is low molecular weight protein, highly conserved, and located in eukaryotic cells[25].All 17 top-rank HSPs genes are a member of low molecular weight (LMW-HSP, 15-30 kDa) or small HSPs. The small HSPs are split into six classes based on their cellular compartmentalization, sequence alignments, and immunological cross-reactivity[19]. Class I, II, and III are localized in the cytoplasm or the nucleus, while the other three (IV, V, VI) are located in the chloroplast, the endoplasmic reticulum, and the mitochondria[26].…”