The orthorhombic SrIrO3 perovskite was synthesized under 5GPa and 1000°C. It is paramagnetic below about 170K and transfers to an unknown magnetism under higher temperature. A band type metal to insulator transition caused by a pseudogap was observed at about 44K. Interestingly a positive magnetoresistance, i.e., resistance increased with applying magnetic field, was observed in the orthorhombic SrIrO3 perovskite below about 170K.

BackgroundHistone acetyltransferases (HATs) play an important role in eukaryotic transcription. Eight HATs identified in rice (OsHATs) can be organized into four families, namely the CBP (OsHAC701, OsHAC703, and OsHAC704), TAFII250 (OsHAF701), GNAT (OsHAG702, OsHAG703, and OsHAG704), and MYST (OsHAM701) families. The biological functions of HATs in rice remain unknown, so a comprehensive protein sequence analysis of the HAT families was conducted to investigate their potential functions. In addition, the subcellular localization and expression patterns of the eight OsHATs were analyzed.ResultsOn the basis of a phylogenetic and domain analysis, monocotyledonous CBP family proteins can be subdivided into two groups, namely Group I and Group II. Similarly, dicotyledonous CBP family proteins can be divided into two groups, namely Group A and Group B. High similarities of protein sequences, conserved domains and three-dimensional models were identified among OsHATs and their homologs in Arabidopsis thaliana and maize. Subcellular localization predictions indicated that all OsHATs might localize in both the nucleus and cytosol. Transient expression in Arabidopsis protoplasts confirmed the nuclear and cytosolic localization of OsHAC701, OsHAG702, and OsHAG704. Real-time quantitative polymerase chain reaction analysis demonstrated that the eight OsHATs were expressed in all tissues examined with significant differences in transcript abundance, and their expression was modulated by abscisic acid and salicylic acid as well as abiotic factors such as salt, cold, and heat stresses.ConclusionsBoth monocotyledonous and dicotyledonous CBP family proteins can be divided into two distinct groups, which suggest the possibility of functional diversification. The high similarities of protein sequences, conserved domains and three-dimensional models among OsHATs and their homologs in Arabidopsis and maize suggested that OsHATs have multiple functions. OsHAC701, OsHAG702, and OsHAG704 were localized in both the nucleus and cytosol in transient expression analyses with Arabidopsis protoplasts. OsHATs were expressed constitutively in rice, and their expression was regulated by exogenous hormones and abiotic stresses, which suggested that OsHATs may play important roles in plant defense responses.

The lattice and electronic and magnetic transport properties of the antiperovskite structure Mn3Zn1−xGexN compounds were investigated. For Mn3ZnN, there is a magnetic transition from antiferromagnetic to paramagnetic near 185K. Correspondingly, the resistivity shows an abrupt drop, but any sudden change of lattice parameters is not found. However, it is interesting that the partial substitution of Ge for Zn induces a lattice contraction near the magnetic transition temperature, where a drop of the resistivity remain, and the transition temperature point increases and the temperature range is broadened with increasing doped Ge contents. The thermodynamics properties were also investigated.