Reversible Double Nucleophilic Substitution Reaction inside Single-Crystal MOF Tuned Remarkable Magnetic Behavior.

Chemical reactions inside single crystals are highly selective but quite challenging. We present herein an octahedral cobalt-oxygen chain-based 3D coordination network with sqc3868 topology, which underwent a reversible double nucleophilic substitution inside a single crystal involving encapsulated DMF molecules and was converted into a topologically highly related frl network, accompanied by magnetic tuning from antiferromagnetism to ferromagnetism. Combined UV-vis, XPS, EPR, and XANES showed most of the Co centers keep a divalent state with less remarkable electronic structure change during the substitution reaction, indicating magnetic tunability mainly comes from a minor change of local geometry of cobalt atoms with large anisotropy.

Enhanced Catalysis Activity in a Coordinatively Unsaturated Cobalt-MOF Generated via Single-Crystal-to-Single-Crystal Dehydration.

Hydrothermal reaction of Co(NO3)2 and terphenyl-3,2",5",3'-tetracarboxyate (H4tpta) generated Co3(OH)2 chains based 3D coordination framework Co3(OH)2(tpta)(H2O)4 (1) that suffered from single-crystal-to-single-crystal dehydration by heating at 160 °C and was transformed into dehydrated Co3(OH)2(tpta) (1a). During the dehydration course, the local coordination environment of part of the Co atoms was transformed from saturated octahedron to coordinatively unsaturated tetrahedron. Heterogenous catalytic experiments on allylic oxidation of cyclohexene show that dehydrated 1a has 6 times enhanced catalytic activity than as-synthesized 1 by using tert-butyl hydroperoxide (t-BuOOH) as oxidant. The activation energy for the oxidation of cylcohexene with 1a catalyst was 67.3 kJ/mol, far below the value with 1 catalysts, which clearly suggested that coordinatively unsaturated Co(II) sites in 1a have played a significant role in decreasing the activation energy. It is interestingly found that heterogeneous catalytic oxidation of cyclohexene in 1a not only gives the higher conversion of 73.6% but also shows very high selectivity toward 2-cyclohexene-1-one (ca. 64.9%), as evidenced in high turnover numbers (ca. 161) based on the open Co(II) sites of 1a catalyst. Further experiments with a radical trap indicate a radical chain mechanism. This work demonstrates that creativity of coordinatively unsaturated metal sites in MOFs could significantly enhance heterogeneous catalytic activity and selectivity.

LlSR28 is involved in pollen germination by affecting filamentous actin dynamics.

Alternative splicing plays important roles in gene regulation and contributes to protein complexity. Previous studies suggest that alternative splicing exists in members of the villin/gelsolin/fragmin superfamily. In this study, a serine/argine-rich (SR) protein cDNA with 28 kDa protein (LlSR28) was isolated from a lily (Lilium longiflorum) expression library. Protein domain analysis showed that LlSR28 had similar structures to Arabidopsis SR45 (AtSR45), and LlSR28 could complement the phenotype of loss of AtSR45 function. Therefore, overexpression of LlSR28 and AtSR45 mutant (atsr45-1) were used in the following experiments. Overexpression of LlSR28 in Arabidopsis completely inhibited pollen germination. In contrast, the pollen germination of atsr45-1 was earlier than that of wild-type. In addition, pollen of atsr45-1 contained less F-actin at the corresponding hydration stage during pollen germination compared to that of wild-type. Alternative splicing analysis showed that Arabidopsis villin1 (AtVLN1) transcript encoding the full-length protein was increased, and that encoding the truncated protein was decreased in atst45-1. Moreover, the mRNA expression level of other actin-binding proteins (ABPs) abundant in Arabidopsis pollen was also changed in atsr45-1. In conclusion, we hypothesize that LlSR28 alters F-actin dynamics probably through its alternative splicing activities to affect directly or indirectly the alternative splicing of AtVLN1 and the expression of different ABPs, which then affects the pollen germination.

AtFH8 is involved in root development under effect of low-dose latrunculin B in dividing cells.

Formins have been paid much attention for their potent nucleating activity. However, the connection between the in vivo functions of AtFHs (Arabidopsis thaliana formin homologs) and their effects on actin organization is poorly understood. In this study, we characterized the bundling activity of AtFH8 in vitro and in vivo. Biochemical analysis showed that AtFH8(FH1FH2) could form dimers and bundle preformed actin filaments or induce stellar structures during actin polymerization. Expression of truncated forms of AtFH8 and immunolocalization analysis showed that AtFH8 localized primarily to nuclear envelope in interphase and to the new cell wall after cytokinesis, depending primarily on its N-terminal transmembrane domain. GUS histochemical staining showed AtFH8 was predominantly expressed in Arabidopsis root meristem, vasculature, and outgrowth points of lateral roots. The primary root growth and lateral root initiation of atfh8 could be decreased by latrunculin B (LatB). Analysis of the number of dividing cells in Arabidopsis root tips showed that much fewer dividing cells in Lat B-treated atfh8 plants than wild-type plants, which indicates that AtFH8 was involved in cell division. Actin cytoskeleton in root meristem of atfh8-1 was more sensitive to LatB treatment than that of wild-type. Altogether, our results indicate that AtFH8 is an actin filament nucleator and bundler that functions in cell division and root development.

ABP41 is involved in the pollen tube development via fragmenting actin filaments.

ABP41 is identified as a novel member of plant villin/gelsolin/fragmin superfamily proteins from lily pollen, which binds stoichiometrically to actin filaments and severs them in vitro. To further understand its in-vivo function and the potential molecular mechanisms, biochemical analysis, fluorescence microscopic observation and microinjection assays were performed. Different biochemical measurements showed that ABP41 maintained actin filaments in forms of short F-actin in vitro. Microinjection of ABP41 into pollen tubes could fragment the pre-existing actin filaments, inhibit the velocity of cytoplasmic streaming, and shorten the length of the clear zone of pollen tube. In addition, it was found that the endogenous ABP41 expressing level was dynamically corresponding to the short actin filament structure in pollen at different stages of pollen germination. Our results suggest that ABP41 is involved in the regulation of actin dynamics during the pollen germination process via maintenance of short dynamic actin filaments.

[Profilins in plant cells].

Actin cytoskeleton is one of the major components of cytoskeleton in eukaryotic cells. In response to endogenous cues or external signals, actin filaments undergo quick polymerization and depolymerization with result in rapid reconstruction of actin cytoskeleton. The dynamic rearrangement of actin filaments in cells are regulated by actin-binding proteins. Profilin is a low-molecular-weight, actin-monomer-binding protein ubiquitously presents in organisms ranging from amoebae and fungi up to higher plants and mammals. Besides binding actin, profilin also binds to phosphatidylinositol 4,5-bisphosphate and poly-L-proline. Recent studies suggest that profilin is a multifunctional protein that has positive and negative regulatory effects on actin polymerization and, in certain case, may be involved in signal transduction. We have long been engaged in the studies on characteristic and function of profilin in plant cells, such as the function analysis of Arabidopsis PRF1 and PRF2, and the effects of profilin on the function of forming in modulating actin cytoskeleton. Here, with the combination of our results, we have reviewed the recent progress in profilin research, including its initial finding, biochemical properties, in vivo distribution and functions, as well as its role in signal transduction.