Efficient floral dip transformation method using on Cav.

Yellow cosmos ( Cav.) is a specific flowering plant and considered a suitable genetic engineering model. -mediated plant transformation is commonly used for plant genetic engineering.

RNA-seq data of tea mosquito bugs, antennae.

Tea Mosquito Bug (TMB), (Hemiptera: Miridae) is one of the major pest infesting tea and cocoa plantations worldwide. Developing olfaction-based control methods was urges as an alternative to commonly used but non-environmental friendly chemical pesticides. However, the molecular mechanisms underlying TMB reception mechanism are still lacking.

Mutation of UDP-glucose binding motif residues lead to increased affinity for ADP-glucose in sugarcane sucrose phosphate synthase.

Plant sucrose-phosphate synthase (SPS) contains a glycosyltransferase domain, which specifically catalyzes reactions with the nucleotide sugar uridine diphosphate glucose (UDP-G) as a donor substrate. Unlike plant SPS, bacterial SPS is predicted to bind other nucleotide sugars, such as adenosine diphosphate glucose (ADP-G). This study aimed to identify the UDP-G binding site of sugarcane (Saccharum officinarum) SPS (SoSPS1) and to improve its affinity for ADP-G by site-directed mutagenesis.

Overexpression of Sucrose Phosphate Synthase Enhanced Sucrose Content and Biomass Production in Transgenic Sugarcane.

Sucrose phosphate synthase (SPS) is a key enzyme in sucrose synthesis, which controls sucrose content in plants. This study was designed to examine the efficacy of the overexpression of gene on sucrose accumulation and carbon partitioning in transgenic sugarcane. The overexpression of gene increased SPS activity and sucrose content in transgenic sugarcane leaves.

Identification of UDP-glucose binding site in glycosyltransferase domain of sucrose phosphate synthase from sugarcane (Saccharum officinarum) by structure-based site-directed mutagenesis.

Sucrose phosphate synthase (SPS) is believed to be the key enzyme for controlling the biosynthesis of sucrose. SPSs consist of a functional glycosyltransferase domain that shares conserved residues with the glycosyltransferase domain of sucrose biosynthesis-related protein. The formation of sucrose-6-phosphate is catalyzed by SPS with the transfer of a glycosyl group of uridine diphosphate glucose (UDP-G) as an activated donor sugar to a fructose-6-phosphate as a sugar acceptor.

Purification and characterization of recombinant sugarcane sucrose phosphate synthase expressed in E. coli and insect Sf9 cells: an importance of the N-terminal domain for an allosteric regulatory property.

Sucrose phosphate synthase (SPS) catalyses the transfer of glycosyl group of uridine diphosphate glucose to fructose-6-phosphate to form sucrose-6-phosphate. Plant SPS plays a key role in photosynthetic carbon metabolisms, which activity is modulated by an allosteric activator glucose-6-phosphate (G6P). We produced recombinant sugarcane SPS using Escherichia coli and Sf9 insect cells to investigate its structure-function relationship.

Identification of Chinese cabbage sentrin as a suppressor of Bax-induced cell death in yeast.

Studies into the cell death program termed apoptosis have resulted in new information regarding how cells control and execute their own demise, including insights into the mechanism by which death-preventing factors can inhibit Bax-induced caspase activation. We investigated high temperature stress-induced cell death in Brassica rapa. Using a yeast functional screening from a Brassica rapa cDNA library, the BH5-127 EST clone encoding an apoptotic suppressor peptide was identified.