Compound of 1-hydroxyphenazine (1-OH-PHZ) is an important fungicide in agricultural production. The ranges of 1-OH-PHZ solubilities in dichloromethane at temperature of 278.5-308.5 K and in ethyl acetate, methanol and water at temperature of 278.5-333.5 K were measured using the analytical stirred flask method at barometric pressure. The color of the liquid remained unchanged throughout. The solubilities of 1-OH-PHZ in water, methanol, ethyl acetate and dichloromethane increased orderly and these solubilities also increased with increasing the temperature. The experimental data was correlated by the modified Apelblat equation. The root mean square deviations were all within 0.5% and the maximum relative average deviation was 5.2%. The calculated solubility shows a good relationship with the experimental solubility.
OsMADS32 is a monocot specific MIKC^c type MADS-box gene that plays an important role in regulating rice floral meristem and organs identity, a crucial process for reproductive success and rice yield. However, its underlying mechanism of action remains to be clari fied. Here, we characterized a hypomorphic mutant allele of OsMADS32/CFO1, cfo1-3 and identi fied its function in controlling rice flower development by bioinformatics and protein-protein interaction analysis. The cfo1-3 mutant produces defective flowers,including loss of lodicule identity, formation of ectopic lodicule or hull-like organs and decreased stamen number,mimicking phenotypes related to the mutation of B class genes. Molecular characterization indicated that mis-splicing of OsMADS32 transcripts in the cfo1-3 mutant resulted in an extra eight amino acids in the K-domain of OsMADS32 protein.By yeast two hybrid and bimolecular fluorescence complementation assays, we revealed that the insertion of eight amino acids or deletion of the internal region in the K1 subdomain of Os MADS32 affects the interaction between OsMADS32 with PISTILLATA(PI)-like proteins OsMADS2 and OsMADS4. This work provides new insight into the mechanism by which Os MADS32 regulates rice lodicule and stamen identity, by interaction with two PI-like proteins via its K domain.
