New host record for three scuttle flies, Megaselia flava, M. kanekoi and M. gotoi (Diptera: Phoridae), on the poisonous fungus Amanita ibotengutake (Agaricales: Amanitaceae)

We identified three species of fungivorous scuttle fly –Megaselia flava, M. kanekoi and M. gotoi– from eight fruit bodies of a fungus, Amanita ibotengutake, which has not previously been recorded as the host of these flies.     

Analysing disparity by applying combined morphological and molecular approaches to French and Japanese carabid beetles

The expression of morphological disparity within a clade is related to its history and to the environmental parameters within which it develops. Recent developments in geometric morphometries allow quantitative estimation of morphological disparity, and facilitate comparisons with genetic data intended to provide phylogenetic information. Such comparisons were made between two sets of ground beetle species from regions that differ biogeographically and environmentally: 12 post-glacial reinvading species from NE France; and 15 Japanese species less likely to be affected by the Pleistocene glacial events. Genetic relationships were inferred from mitochondrial DNA (ND5 gene). Morphological divergences among the species were analysed using Procrustes ver. 2.0, based on 64 landmarks (generalized analyses and computation of additive distance trees). The established morphospaces indicate distinct disparity patterns in France and Japan, even though the genetic data show that neither of the two sets arc monophyletic, and that they are in fact intermixed in the same clade. This discrepancy is partly related to the presence of extreme (elongated) morphologies in the Japanese set. But the stronger disparity observed amongjapanese species does not correspond to greater genetic differences. Those extreme morphologies appear to be related to the degree of endemicity of the species. The differences between the French and Japanese morphological patterns are discussed in the context of possible geographic factors and climatic changes during the Pleistocene.     

Protein synthesis in isolated cell nuclei

1. Nuclei prepared from calf thymus tissue in a sucrose medium actively incorporate labelled amino acids into their proteins. This is an aerobic process which is dependent on nuclear oxidative phosphorylation. 2. Evidence is presented to show that the uptake of amino acids represents nuclear protein synthesis. 3. The deoxyribonucleic acid of the nucleus plays a role in amino acid incorporation. Protein synthesis virtually ceases when the DNA is removed from the nucleus, and uptake resumes when the DNA is restored. 4. In the essential mechanism of amino acid incorporation, the role of the DNA can be filled by denatured or partially degraded DNA, by DNAs from other tissues, and even by RNA. Purine and pyrimidine bases, monoribonucleotides, and certain dinucleotides are unable to substitute for DNA in this system. 5. When the proteins of the nucleus are fractionated and classified according to their specific activities, one finds the histones to be relatively inert. The protein fraction most closely associated with the DNA has a very high activity. A readily extractable ribonucleoprotein complex is also extremely active, and it is tempting to speculate that this may be an intermediary in nucleocytoplasmic interaction. 6. The isolated nucleus can incorporate glycine into nucleic acid purines, and orotic acid into the pyrimidines of its RNA. Orotic acid uptake into nuclear RNA requires the presence of the DNA. 7. The synthesis of ribonucleic acid can be inhibited at any time by a benzimidazole riboside (DRB) (which also retards influenza virus multiplication (11)). 8. The incorporation of amino acids into nuclear proteins seems to require a preliminary activation of the nucleus. This can be inhibited by the same benzimidazole derivative (DRB) which interferes with RNA synthesis, provided that the inhibitor is present at the outset of the incubation. DRB added 30 minutes later has no effect on nuclear protein synthesis. These results suggest that the activation of the nucleus so that it actively incorporates amino acids into its proteins requires a preliminary synthesis of ribonucleic acid. 9. Together with earlier observations (27, 28) on the incorporation of amino acids by cytoplasmic particulates, these results show that protein synthesis can occur in both nucleus and cytoplasm.     

Studies on flower color in Chrysanthemum morifolium RAMAT. I. Anthocyanins

Isolation and characterization of anthocyanins from the flowersof two cultivars of Chrysanthemum morifolium RAMAT. are reported.The main pigment is a new glucoside of cyanidin. ¹Cultivated at the Kyoto University Agricultural ExperimentalFarm (Received October 25, 1969; )     

A Monoclonal Antibody that Binds Preferentially to Human Suppressor T Cells

A monoclonal antibody termed JM3-3-3A was produced by somatic cell hybridization. The reactivity was assessed by indirect immunofluorescence. JM3-3-3A was reactive with 41% human peripheral blood T cells and 48% non-T cells. Among various human lymphoblastoid cell lines (MOLT 4F, JM, and TALL-I), TALL-I was found not to be reactive with JM-13-3-3A. Human peripheral blood Tcells fractionated by JM3-3-3A-coated dish panning were submitted to functional studies. JM3-3-3A positive T cells responded to mitogens, concanavalin A and phytohemagglutinin-P much better than JM3-3-3A negative T cells in the presence or absence of adherent cells. JM3-3-3A positive T cells showed suppressor activity and JM3-3-3A negative T cells showed helper activity in pokeweed mitogen-induced Ig production. More than fifty percent of the JM3-3-3A positive T cells were reactive with OKT8 which binds to suppressor/ cytotoxic T cells, whereas 18% of JM3-3-3A negative T cells were reactive with OKTIl. In addition, immunoprecipitation experiments identified a protein with an approximate molecular weight of 43,000 as a cell surface antigen for JM3-3-3A. Thus, the reactivity of JM3-3-3A showed a wide distribution but human peripheral blood T cells could be dissected functionally by this antibody.