Differential expression of leaf proteins in four cultivars of peanut (Arachis hypogaea L.) under water stress

Abstract

Drought is a major constraint to the productivity of many crops affecting various physiological and biochemical processes. Seventy percent of the peanuts are grown in semiarid tropics that are frequently prone to drought stress. So, we analyzed its effect in 4 cultivars of peanut, with different degrees of drought tolerance, under 10 and 20 days of water stress using two-dimensional gel electrophoresis and mass spectrometry. A total of 189 differentially expressed protein spots were identified in the leaf proteome of all the 4 cultivars using PD Quest Basic software; 74 in ICGV 91114, 41 in ICGS 76, 44 in J 11 and 30 in JL 24. Of these, 30 protein spots were subjected to in-gel trypsin digestion followed by MALDI-TOF that are functionally categorized into 5 groups: molecular chaperones, signal transducers, photosynthetic proteins, defense proteins and detoxification proteins. Of these, 12 proteins were sequenced. Late embryogenesis abundant protein, calcium ion binding protein, sucrose synthase isoform-1, 17.3 kDa heat shock protein and structural maintenance of chromosome proteins were overexpressed only in the 15 and 20 days stressed plants of ICGV 91114 cultivar while cytosolic ascorbate peroxidase was expressed with varying levels in the 10 and 20 days stressed plants of all the 4 cultivars. Signaling protein like 14-3-3 and defense proteins like alpha-methyl-mannoside-specific lectin and mannose/glucose-binding lectins were differentially expressed in the 4 cultivars. Photosynthetic protein like Rubisco was down-regulated in the stressed plants of all 4 cultivars while Photosystem-I reaction center subunit-II of chloroplast precursor protein was overexpressed in only 20 days stressed plants of ICGV 91114, ICGS 76 and J11 cultivars. These differentially expressed proteins could potentially be used as protein markers for screening the peanut germplasm and further crop improvement.

Genomic signatures of the evolution of defence against its natural enemies in the poisonous and medicinal plant Datura stramonium (Solanaceae)

“…A notable domain, the SNF1-related protein kinase regulatory subunit beta-2 (IPR030070) was detected in proteins with physicochemical divergence (Supplementary Tables S9 , S15 online). This domain has been implicated in the response against drought, and in the efficiency of carbohydrate metabolism and in the response to glucose limitation 46 , 47 . Also, we found over-represented domains in proteins with signal of expansion and with positively selected codons containing Galactose oxidase/kelch, beta-propeller (IPR011043) domain (Supplementary Table S15 online).…”

Physiological and Differential Proteomic Analyses of Imitation Drought Stress Response in Sorghum bicolor Root at the Seedling Stage

“…As a technique, proteomics is advantaged over other "omics" tools since proteins are the key players in the majorities of cellular events [18]. Proteomics is the best available molecular tool for understanding the complex molecular mechanism in response to drought stress [19][20][21][22] and has been applied to research on drought stress in rice, maize, wheat, barley, peanut, and so on [12,[23][24][25][26][27][28][29][30].…”

Glycopattern Alteration of Glycoproteins in Gastrointestinal Cancer Cell Lines and Their Cell-Derived Exosomes

“…Lectins are sugar-binding proteins which are highly specific for their sugar moieties purified from various plants, invertebrates, and higher animals. Lectins from different sources can specifically recognize diverse sugar chain structures and mediate a variety of biological processes. , In this study, we performed lectin microarrays to detect glycopattern of glycoproteins of exosomes and cells, respectively. The most significant advantage of lectin microarrays is that only a minimum amount of sample is required to perform simultaneous quantitative analysis of N-linked glycans and O-linked glycans in a complete biological structure without the need to release glycans, which ensures that the most real situation of protein glycosylation in the sample is correctly reflected. − In our research, experiments were carried out by using 20 different lectins.…”