Factors affecting the rapid changes of protein under short-term heat stress
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ABSTRACT:
PROVIDER: PRJNA663325 | ENA |
REPOSITORIES: ENA
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| SRR12637883_1.fastq.gz | Fastqsanger.gz | |||
| SRR12637883_2.fastq.gz | Fastqsanger.gz | |||
| SRR12637884_1.fastq.gz | Fastqsanger.gz | |||
| SRR12637884_2.fastq.gz | Fastqsanger.gz | |||
| SRR12637885_1.fastq.gz | Fastqsanger.gz |
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Project description:The protein content determines the cell state. The variation in protein abundance is crucial when organisms are in the early stages of heat stress, but the reasons affecting their changes are still unknown. We quantified 47,535 mRNAs and 3,742 proteins in filling grain of wheat under two thermal environments. The impact of mRNA abundance and sequence features implicated in protein translation and degradation on protein expression were evaluated by regression analysis. Transcription, codon usage and amino acid frequency mainly affect protein expression, and their combined contribution explains 58.2% and 66.4% of protein abundance variation in two types of heat stresses. Of which, transcription contributes more to the protein expression under severe heat stress (31%) than to mild stress (6%). Codon usage plays a stable and powerful role in protein expression under heat stress, even surpassing transcription. What’s more, the usage of AAG is a key factor regulating rapid protein expression under heat stress. This study revealed the main factors affecting the changes of protein abundance in the early stage of heat stress, and explained the mystery that plants can express protein rapidly under heat stress.
2021-03-23 | GSE157909 | GEO
Project description:BackgroundProtein content determines the state of cells. The variation in protein abundance is crucial when organisms are in the early stages of heat stress, but the reasons affecting their changes are largely unknown.ResultsWe quantified 47,535 mRNAs and 3742 proteins in the filling grains of wheat in two different thermal environments. The impact of mRNA abundance and sequence features involved in protein translation and degradation on protein expression was evaluated by regression analysis. Transcription, codon usage and amino acid frequency were the main drivers of changes in protein expression under heat stress, and their combined contribution explains 58.2 and 66.4% of the protein variation at 30 and 40 °C (20 °C as control), respectively. Transcription contributes more to alterations in protein content at 40 °C (31%) than at 30 °C (6%). Furthermore, the usage of codon AAG may be closely related to the rapid alteration of proteins under heat stress. The contributions of AAG were 24 and 13% at 30 and 40 °C, respectively.ConclusionIn this study, we analyzed the factors affecting the changes in protein expression in the early stage of heat stress and evaluated their influence.
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Project description:In order to study in detail short and mid term heat stress molecular response we performed a shotgun proteomics study. One-year-old P. radiata seedlings (plant size ∼33 ± 4 cm) were kept in 1 dm3 pots under a photoperiod of 16 h (400 µmol m−2 s−1) at 25 °C and 50% relative humidity (RH), and 15 °C and 60% RH during the night period. The plants were previously acclimated over a 1-month period inside the climate chamber, being watered with nutritive solution (N : P : K, 5 : 8 : 10). In order to perform a realistic experiment, and corresponding with the dawn, heat exposure treatment began with an increasing temperature gradient from 15 to 40 °C over 5 h, which was then maintained for 6 h; after that, temperature was gradually decreased from 40 to 15 °C over 5 h. This experimental procedure was repeated for 5 days and sampling was performed at: 3 h after 40 °C was reached on Day 1 (T1/2) and at the end of the 6 h heat exposure on Day 1 (T1), Day 2 (T2), Day 3 (T3) and Day 5 (T5) (Figure 1a). Plants were watered every day to 80% full capacity (FC) in order to avoid a collateral drought stress. A group of control plants was also collected on Day 1 (C) before starting the heat exposure.
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Project description:Heat stress drastically affects anther tissues resulting in poor plant fertility, necessitating an urgent need to determine the key proteins associated in the response of anthers to heat stress. Employing quantitative proteome analysis, we identified several cultivar-specific protein alterations in anthers of Moroberekan (Japonica, heat sensitive), IR64 (Indica, moderately heat tolerant), and Nagina 22 (Aus, heat tolerant) rice types following short-term (ST_HS; one cycle of 42°C, 4 hours before anthesis) and long-term (LT_HS; 6 cycles of 38°C, 6 hours before anthesis) heat treatments. The protein numbers were higher in Nagina 22 than IR 64 and Moroberekan anthers under unstressed and heat stress. The proteins upregulated in long-term heat stress in Nagina 22 were enriched in biological processes related to unfolded protein binding and carboxylic acid metabolism, including amino acid metabolism. In short-term heat stress, Nagina 22 anthers were enriched in proteins associated with vitamin E biosynthesis while proteins downregulated were related to ribosomal proteins. The expression of Hsp20, DnaJ, and Hsp101 was predominantly observed in Nagina 22. Overall, the heat response in Nagina 22 was associated with its capacity for adequate metabolic control and cellular homeostasis which may be critical for its higher reproductive thermotolerance
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Project description:HOP is a family of cytosolic cochaperones whose molecular role in thermotolerance was quite unknown in eukaryotes and unexplored in plants. In this article, we describe that the three members of the HOP family display a different induction pattern under heat, being HOP3 highly regulated during the challenge and the attenuation period. Despite this tight HOP3 regulation, the analysis of the hop1 hop2 hop3 triple mutant demonstrates that the three AtHOP proteins act redundantly to promote long acquired thermotolerance in Arabidopsis. AtHOPs interact very strongly with HSP90 and part of the bulk of HOP shuttles from the cytoplasm to cytoplasmic foci and to the nucleus in response to heat. Consistent with this latter location, and with the formation of a HOP complex with HsfA1, RNAseq analyses demonstrate that HSR is altered in the hop1 hop2 hop3 triple mutant during the heat stress.In addition, this mutant displays an unusual high accumulation of insoluble and ubiquitinated proteins under heat. These data reveal that HOPs play a main role in two different aspects of the response to heat: the maintenance of protein homeostasis and the proper establishment of the HSR, affecting the plant capacity to acclimate to heat stress for long periods.
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