Mediator structure and conformation change

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Application of the phosphomannose-isomerase/mannose selection system in the Agrobacterium-mediated transformation of Lonicera hypoglauca Miq.

Journal of Plant Biochemistry and Biotechnology - The dried buds of Lonicera hypoglauca Miq. have antipyretic, antidotal and anti-inflammatory properties and as Flos lonicerae are widely used in...     

The oncolytic peptide LTX-315 triggers necrotic cell death

The oncolytic peptide LTX-315 has been designed for killing human cancer cells and turned out to stimulate anti-cancer immune responses when locally injected into tumors established in immunocompetent mice. Here, we investigated the question whether LTX-315 induces apoptosis or necrosis. Transmission electron microscopy or morphometric analysis of chromatin-stained tumor cells revealed that LTX-315 failed to induce apoptotic nuclear condensation and rather induced a necrotic phenotype. Accordingly, LTX-315 failed to stimulate the activation of caspase-3, and inhibition of caspases by means of Z-VAD-fmk was unable to reduce cell killing by LTX-315. In addition, 2 prominent inhibitors of regulated necrosis (necroptosis), namely, necrostatin-1 and cycosporin A, failed to reduce LTX-315-induced cell death. In conclusion, it appears that LTX-315 triggers unregulated necrosis, which may contribute to its pro-inflammatory and pro-immune effects.     

Mitogenomic analysis of Montipora cactus and Anacropora matthai (cnidaria; scleractinia; acroporidae) indicates an unequal rate of mitochondrial evolution among Acroporidae corals

The complete nucleotide sequence of the mitochondrial (mt) genome was determined for specimens of the coral species Montipora cactus (Bernard 1897) and Anacropora matthai (Pillai 1973), representing two morphologically distinct genera of the family Acroporidae. These sequences were compared with the published mt genome sequence for the confamilial species, Acropora tenuis (Dana 1846). The size of the mt genome was 17,887 bp and 17,888 bp for M. cactus and A. matthai. Gene content and organization was found to be very similar among the three Acroporidae mt genomes with a group I intron occurring in the NADH dehyrogenase 5 (nad5) gene. The intergenic regions were also similar in length among the three corals. The control region located between the small ribosomal RNA (ms) and the cytochrome oxidase 3 (cox3) gene was significantly smaller in M. cactus and A. matthai (both 627 bp) than in A. tenuis (1086 bp). Only one set of repeated sequences was identified at the 3′-end of the control regions in M. cactus and A. matthai. A lack of the abundant repetitive elements which have been reported for A. tenuis, accounts for the relatively short control regions in M. cactus and A. matthai. Pairwise distances and relative rate analyses of 13 protein coding genes, the group I intron and the largest intergenic region, igr3, revealed significant differences in the rate of molecular evolution of the mt genome among the three species, with an extremely slow rate being seen between Montipora and Anacropora. It is concluded that rapid mt genome evolution is taking place in genus Acropora relative to the confamilial genera Montipora and Anacropora although all are within the relatively slow range thought to be typical of Anthozoa.     

Purification and characterization of RNA polymerase I from a higher plant.

RNA polymerase I was purified from chromatin isolated from auxin-treated soybean hypocotyl. Purification was achieved by using Agarose A-1.5m gel filtration, DEAE-cellulose, CM-sephadex, and phosphocellulose chromatography, and sucrose density gradient centrifugation. With denatured calf thymus DNA as template, the enzyme has a high specific activity (200-300 nmol/mg/30 min at 28 degrees C) which is comparable to other RNA polymerase I enzymes purified from animals and yeast. While the gel profiles indicate that purification to homogeneity (greater than 90%) may not have been achieved, the enzyme appears to be composed of possibly 7 subunits, several of which are similar to the subunits of yeast RNA polymerase I. The putative subunits and molar ratios are 183 000 (1), 136 000 (1), 50 000 (0.5), 46 000 (0.5), 40 000 (0.5), 33 000 (0.2), and 28 000 (2). The purified enzyme strongly prefers a completely denatured template such as poly(dC).