Green leaf volatiles play vital roles in plant biotic stress; however, their functions in plant responses to abiotic stress have not been determined. The aim of this study was to investigate the possible role of (Z)-3-hexeny-1-yl acetate (Z-3-HAC), a kind of green leaf volatile, in alleviating the salinity stress of peanut ( Arachis hypogaea L. ) seedlings and the underlying physiological mechanisms governing this effect. One salt-sensitive and one salt-tolerant peanut genotype were primed with 200 μM Z-3-HAC at the 4-week-old stage before they were exposed to salinity stress. Physiological measurements showed that the primed seedlings possessed higher relative water content, net photosynthetic rate, maximal photochemical efficiency of photosystem II, activities of the antioxidant enzymes, and osmolyte accumulation under salinity conditions. Furthermore, the reactive oxygen species, electrolyte leakage, and malondialdehyde content in the third fully expanded leaves were significantly lower than in nonprimed plants. Additionally, we found that application of Z-3-HAC increased the total length, surface area, and volume of the peanut roots under salinity stress. These results indicated that the green leaf volatile Z-3-HAC protects peanut seedlings against damage from salinity stress through priming for modifications of photosynthetic apparatus, antioxidant systems, osmoregulation, and root morphology.

Human tissue factor pathway inhibitor-2 (hTFPI-2) is a 32-kDa serine protease inhibitor that is associated with the extracellular matrix. hTFPI-2 inhibits several extracellular matrix-degrading serine proteases and may play a role in tumor invasion and metastasis. To study the signal transduction pathway that leads to the activation of the hTFPI-2, we cloned the potential promoter region of this gene adjacent to a heterologous luciferase reporter gene. Phorbol 12-myristate 13-acetate (

Phenylketonuria is an inborn error of metabolism caused by loss of function of the liver-expressed enzyme phenylalanine hydroxylase and is characterized by elevated systemic phenylalanine levels that are neurotoxic. Current therapies do not address the underlying genetic disease or restore the natural metabolic pathway resulting in the conversion of phenylalanine to tyrosine. A family of hepatotropic clade F adeno-associated viruses (AAVs) was isolated from human CD34 + hematopoietic stem cells (HSCs) and one (AAVHSC15) was utilized to deliver a vector to correct the phenylketonuria phenotype in Pah enu2 mice. The AAVHSC15 vector containing a codon-optimized form of the human phenylalanine hydroxylase cDNA was administered as a single intravenous dose to Pah enu2 mice maintained on a phenylalanine-containing normal chow diet. Optimization of the transgene resulted in a vector that produced a sustained reduction in serum phenylalanine and normalized tyrosine levels for the lifespan of Pah enu2 mice. Brain levels of phenylalanine and the downstream serotonin metabolite 5-hydroxyindoleacetic acid were restored. In addition, the coat color of treated mice darkened following treatment, indicating restoration of the phenylalanine metabolic pathway. Taken together, these data support the potential of an AAVHSC15-based gene therapy as an investigational therapeutic for phenylketonuria patients.

Understanding the effects of different sowing patterns and densities on plant growth characters and yield of peanut is essential for the design and adjustment of management practices that allow improvement and stabilization of peanut production. In the present study, Arachis hypogaea L. cv. Luhua 11 was used to determine the effects of planting density on pod development and yield of peanuts under the mode of single seeded precision sowing through field experiments. The results showed that an appropriate precision sowing density of 195,000-225,000 per hectare leads to an optimal pod number to produce pods, with dry matter accumulation resulting in significantly increased pod yield and harvest index(HI). When the same area sowing seed number of 255,000 per hectare, the kernel yield, pod yield, and HI per plant of the single seeded precision sowing method were higher than those of the double seeded precision sowing method.

The specificity of the pathway used by Vibrio cholerae for extracellular transport of cholera toxin (CT) and other proteins was examined in several different ways. First, V. cholerae was tested for the ability to secrete the B polypeptides of the type II heat-labile enterotoxins of Escherichia coli. Genes encoding the B polypeptide of LT-IIb in pBluescriptKS ؊ phagemids were introduced into V. cholerae by electroporation. Culture supernatants and periplasmic extracts were collected from cultures of the V. cholerae transformants, and the enterotoxin B subunits were measured by an enzyme-linked immunosorbent assay. Results confirmed that the B polypeptides of both LT-IIa and LT-IIb were secreted by V. cholerae with efficiencies comparable to that measured for secretion of CT. Second, the plasmid clones were introduced into strain M14, an epsE mutant of V. cholerae. M14 failed to transport the B polypeptides of LT-IIa and LT-IIb to the extracellular medium, demonstrating that secretion of type II enterotoxins by V. cholerae proceeds by the same pathway used for extracellular transport of CT. These data suggest that an extracellular transport signal recognized by the secretory machinery of V. cholerae is present in LT-IIa and LT-IIb. Furthermore, since the B polypeptide of CT has little, if any, primary amino acid sequence homology with the B polypeptide of LT-IIa or LT-IIb, the transport signal is likely to be a conformation-dependent motif. Third, a mutant of the B subunit of CT (CT-B) with lysine substituted for glutamate at amino acid position 11 was shown to be secreted poorly by V. cholerae, although it exhibited immunoreactivity and ganglioside G M1-binding activity comparable to that of wild-type CT-B. These findings suggest that Glu-11 may be within or near the extracellular transport motif of CT-B. Finally, the genetic lesion in the epsE allele of V. cholerae M14 was determined by nucleotide sequence analysis.