https://www.selleckchem.com/ Furthermore, the M. incognita reproduction factor was reduced up to 71-, 344-, 107- and 114-fold in Arabidopsis plants expressing Mi-msp3, Mi-msp5, Mi-msp18 and Mi-msp24 dsRNA constructs, respectively. This study provides a set of potential target genes to curb nematode infestation in economically important crops via the HD-RNAi approach.Flavonoids are extensively distributed secondary metabolites in land plants. They play a critical role in plant evolution from aquatic to terrestrial and plant adaption to ultraviolet radiation. However, the downstream branching pathway of flavonoids and its regulatory mechanism in bryophytes, which are the most ancient of terrestrial plants, remain unclear. Here, a type I flavone synthase (PnFNSI) was characterized from the Antarctic moss Pohlia nutans. PnFNSI was primarily distributed in the cytoplasm, as detected by subcellular localization. PnFNSI could catalyze the conversion of naringenin to apigenin with an optimal temperature between 15 and 20 °C in vitro. Overexpression of PnFNSI in Arabidopsis alleviated the growth restriction caused by naringenin and accumulated apigenin product. PnFNSI-overexpressing plants showed enhanced plant tolerance to drought stress and UV-B radiation. PnFNSI also increased the enzyme activities and gene transcription levels of reactive oxygen species (ROS) scavengers, protecting plants against oxidative stress. Moreover, overexpression of PnFNSI enhanced the flavone biosynthesis pathway in Arabidopsis. Therefore, this moss FNSI-type enzyme participates in flavone metabolism, conferring protection against drought stress and UV-B radiation.Peruvianin-I is a cysteine peptidase (EC 3.4.22) purified from Thevetia peruviana. Previous studies have shown that it is the only germin-like protein (GLP) with proteolytic activity described so far. In this work, the X-ray crystal structure of peruvianin-I was determined to a resolution of 2.15 Å (PDB accession number 6ORM) and its