Nevada: A new genus for Smelowskia holmgrenii (Brassicaceae)

Nevada holmgrenii was originally described by Rollins as aSmelowskia, but based on phenetic similarities it appears to be more closely related to the arctic/alpine generaBraya andEutrema. It is, however, sufficiently distinct from these genera to be planced in a nonotypic genus,Nevada.     

Vertical Distribution of Three Nematode Genera in a Bentgrass Putting Green in Central Illinois

A study was conducted to determine the vertical distribution of Tylenchorhynchus nudus, Criconemella curvata, and Helicotylynchus cornurus in the upper 5 cm of bentgrass (Agrostis palustris cv. Penncross) putting green turf. The effect of fenamiphos on the vertical distribution of these species also was examined. Experimental design was a split-plot in which whole-plots were fenamiphos treated (0.11 kg a.i./100 m²) or untreated, and sub-plots were two strata (depths of 0-2.5 crn and 2.5-5.0 cm). Soil samples were collected during the growing season for 2 years after treatment to determine root weight and number of nematodes. Root weight was greater in the upper stratum on all sampling dates in both years. When differences between strata in population density were observed, T. nudus, C. curvata, and H. cornurus were more concentrated in the upper stratum. Vertical distribution of T. nudus, C. curvata, and H. cornurus was similar to the distribution of root weight. The difference in population density of H. cornurus between upper and lower strata was affected by fenamiphos on some dates, whereas differences between strata were unaffected for T. nudus and C. curvata. Double arcsine transformed proportions of the total populations of T. nudus, C. curvata, and H. cornurus in the upper stratum on each sampling date indicated no differences between fenamiphos treated and untreated plots in 1989 or 1990.     

Mutations in Rhizobium phaseoli that lead to arrested development of infection threads.

Two Rhizobium phaseoli mutants, isolated previously by Tn5 mutagenesis, elicited infection threads which ceased development prematurely, usually within root hairs. These infection threads were wide, globular, and otherwise altered in morphology, compared with normal infection threads. Anatomy and division of the root cortical cells during initial stages of nodule morphogenesis appeared normal. However, later nodule differentiation deviated considerably from normal development, and release of bacteria from infection threads was not observed. In tryptone-yeast extract medium the mutants sedimented during growth in shaken cultures and formed rough colonies on agar. Electrophoresis of washed cultures solubilized in dodecyl sulfate revealed that the major carbohydrate band was absent from the mutants. The behavior of this carbohydrate in phenol-water extraction and gel chromatography, its apparent ketodeoxyoctonate content, and its susceptibility to mild acid hydrolysis suggested that it was a lipopolysaccharide. From the results of genetic crosses or reversion analysis, the defect in synthesizing this carbohydrate material and the defect in infection could be attributed to a single mutation in each mutant.     

Quantitative high-throughput screening using a live-cell cAMP assay identifies small-molecule agonists of the TSH receptor

The thyroid-stimulating hormone (TSH; thyrotropin) receptor belongs to the glycoprotein hormone receptor subfamily of 7-transmembrane spanning receptors. TSH receptor (TSHR) is expressed mainly in thyroid follicular cells and is activated by TSH, which regulates the growth and function of thyroid follicular cells. Recombinant TSH is used in diagnostic screens for thyroid cancer, especially in patients after thyroid cancer surgery. Currently, no selective small-molecule agonists of the TSHR are available. To screen for novel TSHR agonists, the authors miniaturized a commercially available cell-based cyclic adenosine 3',5' monophosphate (cAMP) assay into a 1536-well plate format. This assay uses an HEK293 cell line stably transfected with the TSHR coupled to a cyclic nucleotide gated ion channel as a biosensor. From a quantitative high-throughput screen of 73,180 compounds in parallel with a parental cell line (without the TSHR), 276 primary active compounds were identified. The activities of the selected active compounds were further confirmed in an orthogonal homogeneous time-resolved fluorescence cAMP-based assay. Forty-nine compounds in several structural classes have been confirmed as the small-molecule TSHR agonists that will serve as a starting point for chemical optimization and studies of thyroid physiology in health and disease.     

Microsatellite Loci of the Cattle Tick Boophilus Microplus (Acari: Ixodidae)

This brief communication reports the identification of microsatellite loci in the economically important tick species Boophilus microplus. The data are potentially useful in distinguishing different strains of B. microplus. Eight polymorphic loci were isolated in larvae, male and female adults analysed individually from 12 field isolates and laboratory strains from Australia (n = 8), Brazil, Mexico, Papua New Guinea and Zimbabwe. Nucleotide sequencing of alleles at these microsatellite loci revealed that non-repeat bases interrupted dinucleotide and tetranucleotide repeats in some loci. Loci with non-repeat bases interrupting them were shorter compared with loci that were not interrupted. Thus the presence of non-repeat bases in a repeated sequence seems to constrain the evolution of additional repeats by slip-strand misparing at these loci.     

Formation of thermally induced aggregates of the soya globulin beta-conglycinin.

The effect of ionic strength (I) on the formation of thermally induced aggregates by the 7S globular storage protein of soya, beta-conglycinin, has been studied using atomic force microscopy. Aggregates were only apparent when I> or =0.1, and had a fibrous appearance, with a height (diameter) of 8-11 nm. At high ionic strength (I=1.0) the aggregates appeared to associate into clumps. When aggregate formation was studied at I=0.2, it was clear that aggregation only began at temperatures above the main thermal transition for the protein at 75 degrees C, as determined by differential scanning calorimetry. This coincided with a small change in secondary structure, as indicated by circular dichroism spectroscopy, suggesting that a degree of unfolding was necessary for aggregation to proceed. Despite prolonged heating the size of the aggregates did not increase indefinitely, suggesting that certain beta-conglycinin isoforms were able to act as chain terminators. At higher protein concentrations (1% w/v) the linear aggregates appeared to form large macroaggregates, which may be the precursors of protein gel formation. The ability of beta-conglycinin to form such distinctive aggregates is discussed in relation to the presence of acidic inserts in certain of the beta-conglycinin subunits, which may play an important role in limiting aggregate length.