The biochemical characteristics and ubiquinones of 44 strains of Trichosporon beigelii and 12 strains of 7 other species of Trichosporon were investigated. The ubiquinone of the genus Trichosporon consist of 4 components: Q-7, Q-8, Q-9, and Q-10, which have different length of isoprenoids in their side chains. The major ubiquinone components in the strains were divided between T. beigelii and the "other species" as follows: In T. beigelii there were 14 strains with Q-10, 29 strains with Q-9 and one with Q-8. In the "other species" all 12 strains had Q-9 as major components. The strains of T. beigelii have been divided into 2 groups: the strains in one group assimilate melibiose and raffinose, the others do not. In the group that assimilates, the major components are: 14 strains, Q-10; 2 strains, Q-9; and 1 strain, Q-8. All strains of T. beigelii that do not assimilate melibiose and raffinose have Q-9 as the major component. These findings suggest that T. beigelii is heterogenous and could be divided into four groups.
Strain AT-25 isolated from a soil sample collected in Japan, showed potent antithrombin activity in its culture filtrate. The strain was a strictly aerobic, gram-positive and pleomorphic rod. The properties of the strain, especially the presence of LL-diaminopimelic acid (LL-DAP), tetrahydrogenated menaquinone with eight isoprene units (MK-8(H4)), and DNA with 72.9mol% of guanine plus cytosine, indicate that strain AT-25 is closely related to Arthrobacter simplex and Arthrobacter tumescens, while these species do not belong to the genus Arthrobacter in strict meaning. The unique characteristics of strain AT-25 are requirement of SO42- for growth and the production of a galactan sulfate with antithrombin activity. The most suitable medium for the production of galactan sulfate was a fermentation medium consisting of 0.05% Na2SO4, 2% glycerol, 0.5% (NH4)2HPO4, 0.1% KH2PO4, and 0.1% yeast extract (pH 7.2).
Eight hybridoma cell clones, obtained by fusing murine myeloma cells (P3-NS1/1-Ag-1) with the spleen cells of immunized BALB/c mice, secreted monoclonal antibodies against the 65-kD mosquitocidal protein of the Bacillus thuringiensis strain PG-14 (flagellar serotype 8a: 8b). Of these monoclonal antibodies, six belonged to the IgM class and two belonged to the IgG1 class. In binding tests, they were all specific for the 65-kD protein and did not react to the 25-kD hemolytic protein produced by the same bacterial strain. Indirect competitive enzyme-linked immunosorbent assays with two monoclonal antibodies (IgM), designated D8C1 and D8B4, had a sensitivity of 1ng/ml for the 65-kD protein. There was no competition by the 25-kD protein.
For the chemotaxonomy of actinomycetes, we describe the optical resolution method for 2, 6-diaminopimelic acid (DAP) stereoisomers by high performance liquid chromatography (HPLC) using 2, 3, 4, 6-tetra-O-acetyl- β-D-glucopyranosyl isothiocyanate (GITC). The analysis was applicable both to whole-cell preparations and to cell wall ones. This method made it possible to analyze quantitatively LL-, DD-, and meso-DAP, compared with the previously reported methods of paper chromatography, thin-layer chromatography and HPLC.
The coupling site of a respiration-dependent primary Na+ pump to the respiratory chain was studied in a psychrophilic bacterium, Vibrio sp. strain ABE-1. Several inhibitory experiments showed that the Na+ extrusion caused by a respiration-dependent primary Na+ pump was not ATP-dependent ion translocations. NaCl stimulated NADH oxidase activity at pH 6.5 but inhibited it at pH 8.5. 2-n-Heptyl-4-hydroxyquinoline N-oxide (HQNO), a respiratory inhibitor that greatly inhibited the primary Na+ pump at pH 6.5 and 8.5, also inhibited the NADH oxidase activity, greatly at pH 6.5 and faintly at pH 8.5. On the other hand, NADH: ubiquinone-1 oxidoreductase activities were stimulated by NaCl to a similar extent at pH 6.5 and 8.5, but in the presence of O.425M NaCl it was inhibited by HQNO at pH 8.5 less than at pH 6.5. These results showed that the primary Na+ pump at pH 6.5 is coupled to NADH: quinone oxidoreductase, and suggested that the coupling site of the pump at pH 8.5 was distinct from the site at pH 6.5.
Extragenic suppressor mutants for the sigA47 (crsA47, rpoD47) mutation were isolated and analyzed. Among 48 spontaneous suppressor mutants (sca), 13 were deficient in sporulation and these mutations were mapped in the spo0A, spo0B, and spo0F genes, respectively. During the mapping studies, spo0G14 and spo0D8 mutations were found to be alleles of the spo0A and spo0B genes, respectively. Thes results indicate that a link exists between the RNA polymerase sigA enzyme, glucose catabolite repression, and some of the spo0 gene functions.
A hitherto undescribed ballistospore-forming yeast was isolated from Knightia excelsa infected by sooty molds collected in New Zealand. It is characterized by ubiquinone-9 and the lack of xylose in the cells so that it is included in the genus Bensingtonia. This yeast resembles B. intermedia and B. yamatoana but is easily distinguished from these two species by the assimilation of nitrate and lactose and the requirement of pyridoxine. Bensingtonia ingoldii Nakase et Itoh sp. nov. is proposed for this yeast.
The calmodulin level in the cell division cycle yeast mutants defective at the G1 and S phases decreased to less than half of that in the wild type during incubation at high (37°C) temperature. The calmodulin levels were elevated twofold in parallel with the budding process during the cell cycle in wild-type cells. These levels decreased after cell duplication, and the G1 daughter cells contained half the maximum calmodulin level found before cell uplication.