A leaf shape mutant provides insight into PINOID Serine/Threonine Kinase function in cucumber(Cucumis sativus L.)

Optimizing leaf shape is a major challenge in efforts to develop an ideal plant type. Cucumber leaf shapes are diverse; however, the molecular regulatory mechanisms underlying leaf shape formation are unknown. In this study, we obtained a round leaf mutant(rl) from an ethyl methanesulfonate-induced mutagenesis population. Genetic analysis revealed that a single recessive gene, rl, is responsible for this mutation. A modified Mut Map analysis combined linkage mapping identified a single nucleotide polymorphism within a candidate gene,Csa1 M537400, as the mutation underlying the trait.Csa1 M537400 encodes a PINOID kinase protein involved in auxin transport. Expression of Csa1 M537400 was significantly lower in the rl mutant than in wild type, and it displayed higher levels of IAA(indole-3-acetic acid) in several tissues. Treatment of wild-type plants with an auxin transport inhibitor induced the formation of round leaves,similar to those in the rl mutant. Altered expression patterns of several auxin-related genes in the rl mutant suggest that rl plays a key role in auxin biosynthesis,transport, and response in cucumber. These findings provide insight into the molecular mechanism underlying the regulation of auxin signaling pathways in cucumber,and will be valuable in the development of an ideal plant type.     

Benchmarking the Activity,Stability, and Inherent Electrochemistry of Amorphous Molybdenum Sulfide for Hydrogen Production

Anodically electrodeposited amorphous molybdenum sulfide (AE‐MoS_x) has attracted significant attention as a non‐noble metal electrocatalyst for its high activity toward the hydrogen evolution reaction (HER). The [Mo₃S₁₃]^2? polymer‐based structure confers a high density of exposed sulfur moieties, widely regarded as the HER active sites. However, their intrinsic complexity conceals full understanding of their exact role in HER catalysis, hampering their full potential for water splitting applications. In this report, a unifying approach is adopted accounting for modifications in the inherent electrochemistry (EC), HER mechanism, and surface species to maximize the AE‐MoS_x electroactivity over a broad pH region (0–10). Dramatic enhancements in HER performance by selective electrochemical cycling within reductive (overpotential shift, η_HER ≈ ?350 mV) and electro‐oxidative windows (η_HER ≈ ?290 mV) are accompanied by highly stable performance in mildly acidic electrolytes. Joint analysis of X‐ray photoelectron spectroscopy, Raman, and EC experiments corroborate the key role of bridging and terminal S ligands as active site generators at low pH, and reveal molybdenum oxysulfides (Mo⁵⁺O_xS_y) to be the most active HER moiety in AE‐MoS_x in mildly acidic‐to‐neutral environments. These findings will be extremely beneficial for future tailoring of MoS_x materials and their implementation in commercial electrolyzer technologies.     

Structural and functional characterization of a novel acidophilic 7α‐hydroxysteroid dehydrogenase

7α‐Hydroxysteroid dehydrogenase (7α‐HSDH) is an NAD(P)H‐dependent oxidoreductase belonging to the short‐chain dehydrogenases/reductases. In vitro, 7α‐HSDH is involved in the efficient biotransformation of taurochenodeoxycholic acid (TCDCA) to tauroursodeoxycholic acid (TUDCA). In this study, a gene encoding novel 7α‐HSDH (named as St‐2‐1) from fecal samples of black bear was cloned and heterologously expressed in Escherichia coli. The protein has subunits of 28.3 kDa and a native size of 56.6 kDa, which suggested a homodimer. We studied the relevant properties of the enzyme, including the optimum pH, optimum temperature, thermal stability, activators, and inhibitors. Interestingly, the data showed that St‐2‐1 differs from the 7α‐HSDHs reported in the literature, as it functions under acidic conditions. The enzyme displayed its optimal activity at pH 5.5 (TCDCA). The acidophilic nature of 7α‐HSDH expands its application environment and the natural enzyme bank of HSDHs, providing a promising candidate enzyme for the biosynthesis of TUDCA or other related chemical entities.     

Lipidomic Analysis of α-Synuclein Neurotoxicity Identifies Stearoyl CoA Desaturase as a Target for Parkinson Treatment

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Unbalanced biparental care during colony foundation in two subterranean termites

Parental care is a major component of reproduction in social organisms, particularly during the foundation steps. Because investment into parental care is often costly, each parent is predicted to maximize its fitness by providing less care than its partner. However, this sexual conflict is expected to be low in species with lifelong monogamy, because the fitness of each parent is typically tied to the other's input. Somewhat surprisingly, the outcomes of this tug‐of‐war between maternal and paternal investments have received important attention in vertebrate species, but remain less known in invertebrates. In this study, we investigated how queens and kings share their investment into parental care and other social interactions during colony foundation in two termites with lifelong monogamy: the invasive species Reticulitermes flavipes and the native species R. grassei. Behaviors of royal pairs were recorded during six months using a non‐invasive approach. Our results showed that queens and kings exhibit unbalanced investment in terms of grooming, antennation, trophallaxis, and vibration behavior. Moreover, both parents show behavioral differences toward their partner or their descendants. Our results also revealed differences among species, with R. flavipes exhibiting shorter periods of grooming and antennation toward eggs or partners. They also did more stomodeal trophallaxis and less vibration behavior. Overall, this study emphasizes that despite lifelong monogamy, the two parents are not equally involved in the measured forms of parental care and suggests that kings might be specialized in other tasks. It also indicates that males could play a central, yet poorly studied role in the evolution and maintenance of the eusocial organization.     

Hu proteins regulate polyadenylation by blocking sites containing U-rich sequences

A recent genome-wide bioinformatic analysis indicated that 54% of human genes undergo alternative polyadenylation. Although it is clear that differential selection of poly(A) sites can alter gene expression, resulting in significant biological consequences, the mechanisms that regulate polyadenylation are poorly understood. Here we report that the neuron-specific members of a family of RNA-binding proteins, Hu proteins, known to regulate mRNA stability and translation in the cytoplasm, play an important role in polyadenylation regulation. Hu proteins are homologs of the Drosophila embryonic lethal abnormal visual protein and contain three RNA recognition motifs. Using an in vitro polyadenylation assay with HeLa cell nuclear extract and recombinant Hu proteins, we have shown that Hu proteins selectively block both cleavage and poly(A) addition at sites containing U-rich sequences. Hu proteins have no effect on poly(A) sites that do not contain U-rich sequences or sites in which the U-rich sequences are mutated. All three RNA recognition motifs of Hu proteins are required for this activity. Overexpression of HuR in HeLa cells also blocks polyadenylation at a poly(A) signal that contains U-rich sequences. Hu proteins block the interaction between the polyadenylation cleavage stimulation factor 64-kDa subunit and RNA most likely through direct interaction with poly(A) cleavage stimulation factor 64-kDa subunit and cleavage and polyadenylation specificity factor 160-kDa subunit. These studies identify a novel group of mammalian polyadenylation regulators. Furthermore, they define a previously unknown nuclear function of Hu proteins.