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Soybean (Glycine max[Linn.] Merr.) is an important oilseed crop. Although transcription factors (TFs) can coordinate the expression of mRNA and lncRNA, their coordination in the soybean oil synthesis pathway remains unclear. This study examined the interaction between the TF GmDof11 and lncRNA13082and found that overexpression of GmDof11led to an increase in the number of Arabidopsisseeds, thousand seed weight, crude protein, hydrolysis amino acid, and soluble sugar. Additionally, it reduced the triglyceride and starch contents and affected the proportion of fatty acids, increasing the contents of palmitic acid, stearic acid, and linolenic acid. The yeast two-hybrid experiments revealed that GmDof11 interacts with GmBCCP1, GmLEC1b, and GmFAB2 proteins. In the RT-qPCR analysis of transgenic soybean roots, it was found that GmDof11 can activate the production of lncRNA13082and work in conjunction with lncRNA13082to oversee oil synthesis and nutrient storage. Our research provides robust theoretical evidence for a comprehensive resolution of TF-lncRNAregulation in the soybean oil synthesis network.

Both adsorbed and free water occur in shale matrix pores and intensely impact methane accumulation and transport in a shale gas reservoir. As a result of multiple water coexistence in complicated nanoporous shale, there still is a large challenge for the determination of the storage capacities and microdistributions of adsorbed and free water. In this study, storage characteristics of adsorbed and free water in deep gas-producing shales from the southern Sichuan Basin of China were investigated using a collaborative evaluation of centrifugation and nuclear magnetic resonance (NMR) under atmospheric pressure and 30 °C temperature conditions. Results show the following: (1) The amounts of adsorbed and free water in water-saturated shales are 1.7967–16.0964 mg/g (mean of 9.3875 mg/g) and 6.4267–19.8020 mg/g (mean of 11.0377 mg/g), respectively. The adsorbed water accounts for 15.83–66.10 wt % (mean of 45.14 wt %) of total water. Adsorbed water mainly exists in pores developed in solid bitumen and clay mineral. More free water is stored in the pores of solid bitumen than that in clay mineral-related pores. (2) The adsorbed water primarily distributes in pores of <20 nm; in contrast, the free water is mainly stored in >2 nm pores. The microdistributions of adsorbed and free water were controlled by the pore size distribution in shales. The mass ratio of adsorbed water decreases with increasing the pore size. (3) The presence of adsorbed water implies that some of water stored in matrix pores cannot flow. The free water is a potential source of the flowback fluid of the shale gas well. This study not only provides an evaluation theory and method but also contributes to insight into the gas–water storage in shale pores.

Both synthetic and endogenous glucocorticoids are important pharmaceutic drugs known to bind to the ligand-binding domain (LBD) of glucocorticoid receptor (GR), a member of the nuclear receptor (NR) superfamily. Ligand binding induces conformational changes within GR, resulting in subsequent DNA binding and differential coregulator recruitment, ultimately activating or repressing target gene expression. One of the most crucial coregulators is peroxisome proliferator-activated γcoactivator 1-α(PGC1α), which acts to regulate energy metabolism by directly interacting with GR to modulate gene expression. However, the mechanisms through which PGC1αsenses GR conformation to drive transcription are not completely known. Here, an ancestral variant of the GR (AncGR2) LBD was used as a tool to produce stable protein for biochemical and structural studies. PGC1αis found to interact more tightly and form a more stable complex with AncGR2 LBD than nuclear receptor coactivator 2. We report the first high-resolution X-ray crystal structures of AncGR2 LBD in complex with PGC1αand dexamethasone (DEX) or hydrocortisone (HCY). Structural analyses reveal how distinct steroid drugs bind to GR with different affinities by unique hydrogen bonds and hydrophobic interactions. Important charge clamps are formed between the activation function 2 and PGC1αto mediate their specific interactions. These interactions lead to a high level of protection from hydrogen-deuterium exchange at the coregulator interaction site and strong intramolecular allosteric communication to ligand binding site. This is the first structure detailing the GR–PGC1αinteraction providing a foundation for future design of specific therapeutic agents targeting these critical metabolic regulators.SIGNIFICANCE STATEMENTHigh-resolution structures of AncGR2 LBD bound to DEX and HCY in complex with PGC1α reveal the molecular mechanism of PGC1α binding to AncGR2 LBD as well as the distinct affinities between DEX and HCY binding. Identifying the structural mechanisms that drive drug affinity is of pharmacologic interest to the glucocorticoid receptor field as an avenue to guide future drug design targeting GR-PGC1α signaling, which plays a crucial role in controlling hepatic glucose output.