Dual conformational recognition by Z-DNA binding protein is important for the B-Z transition process.

Left-handed Z-DNA is radically different from the most common right-handed B-DNA and can be stabilized by interactions with the Zα domain, which is found in a group of proteins, such as human ADAR1 and viral E3L proteins. It is well-known that most Zα domains bind to Z-DNA in a conformation-specific manner and induce rapid B-Z transition in physiological conditions. Although many structural and biochemical studies have identified the detailed interactions between the Zα domain and Z-DNA, little is known about the molecular basis of the B-Z transition process. In this study, we successfully converted the B-Z transition-defective Zα domain, vvZαE3L, into a B-Z converter by improving B-DNA binding ability, suggesting that B-DNA binding is involved in the B-Z transition. In addition, we engineered the canonical B-DNA binding protein GH5 into a Zα-like protein having both Z-DNA binding and B-Z transition activities by introducing Z-DNA interacting residues. Crystal structures of these mutants of vvZαE3L and GH5 complexed with Z-DNA confirmed the significance of conserved Z-DNA binding interactions. Altogether, our results provide molecular insight into how Zα domains obtain unusual conformational specificity and induce the B-Z transition.

Comparative study of the quality characteristics of defatted soy flour treated by supercritical carbon dioxide and organic solvent.

Defatted soy flour is a potential source of food protein, amino acids, ash and isoflavones. The supercritical carbon dioxide (SC-CO2) and a traditional organic solvent extraction methods were used to remove fat from soy flour, and the quality characteristics of a control soy flour (CSF), defatted soy flour by SC-CO2 (DSFSC-CO2) and defatted soy flour by an organic solvent (DSF-OS) were compared. The SC-CO2 process was carried out at a constant temperature of 45 °C, and a pressure of 40 MPa for 3 h with a CO2 flow rate of 30 g/min. The DSFSC-CO2 had significantly higher protein, ash, and amino acids content than CSF and DSF-OS. The sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) analysis demonstrated that CSF and DSFSC-CO2 had protein bands of similar intensity and area that indicated no denaturation of protein, whereas DSF-OS showed diffuse bands or no bands due to protein denaturation. In addition to higher nutritional value and protein contents, DSFSC-CO2 showed superior functional properties in terms of total soluble solids content, water and oil absorption, emulsifying and foaming capacity. The SC-CO2 method offers a nutritionally and environmentally friendly alternative extraction processing approach for the removal of oil from high-protein food sources. It has a great potential for producing high-protein fat-free, and low-calorie content diet than the traditional organic solvent extraction method.