Inheritance of resistance to neonatal E. coli diarrhoea in the pig: examination of the genetic system

Summary Evidence is presented that a dominant allele, S, is expressed as a receptor for K88 on the brushborder surface of the pig intestinal cell. The homozygous recessive (ss) lacks this receptor. The receptor enables K88 — positive coliforms to adhere to the gut of the piglet which they must do if they are to cause neonatal diarrhoea. The homozygous recessive is thus a disease resistant animal.A possible reason for the persistence of the dominant (susceptible) gene is given.     

Greater phosphorus uptake in forested headwater streams modified by clearfell forestry

Clearfell, burn and sow (CBS) forestry can potentially alter stream environments by increasing available light and the input of woody debris. However, little is known about how CBS forestry affects in-stream processes such as nutrient uptake. We evaluate whether short-term (2–7 years) environmental changes (e.g. light availability and woody debris) associated with CBS forestry lead to differences in nutrient uptake metrics. To do this, we measured in-stream uptake of soluble reactive phosphorus (SRP) and ammonium (NH₄) in three old growth (OG) and four CBS-affected headwater stream reaches. The abundance of fine woody debris and light availability were significantly greater in CBS-affected than in OG reaches. Uptake velocities varied from 0.0880 to 0.951 mm min^?1 for NH₄ and from 0.0383 to 1.06 mm min^?1 for SRP across all sites. The mean uptake of SRP, but not NH₄, was significantly greater (i.e. higher uptake velocities and lower uptake lengths) in CBS-affected than in OG reaches. These results suggest that CBS forestry altered the stream environment enabling greater SRP uptake relative to OG reaches. Our findings highlight the tight linkage between headwater streams and their surrounding terrestrial environment, which has direct implications for catchment-scale biogeochemical processes.     

Temperature and Electrolyte Optimization of the α-Hemolysin Latch Sensing Zone for Detection of Base Modification in Double-Stranded DNA

The latch region of the wild-type protein pore α-hemolysin (α-HL) constitutes a sensing zone for individual abasic sites (and furan analogs) in double-stranded DNA (dsDNA). The presence of an abasic site or furan within a DNA duplex, electrophoretically captured in the α-HL vestibule and positioned at the latch region, can be detected based on the current blockage prior to duplex unzipping. We investigated variations in blockage current as a function of temperature (12–35°C) and KCl concentration (0.15–1.0 M) to understand the origin of the current signature and to optimize conditions for identifying the base modification. In 1 M KCl solution, substitution of a furan for a cytosine base in the latch region results in an ∼8 kJ mol⁻¹ decrease in the activation energy for ion transport through the protein pore. This corresponds to a readily measured ∼2 pA increase in current at room temperature. Optimal resolution for detecting the presence of a furan in the latch region is achieved at lower KCl concentrations, where the noise in the measured blockage current is significantly lower. The noise associated with the blockage current also depends on the stability of the duplex (as measured from the melting temperature), where a greater noise in the measured blockage current is observed for less stable duplexes.     

Unusual Isothermal Hysteresis in DNA i-Motif pH Transitions: A Study of the RAD17 Promoter Sequence

We have interrogated the isothermal folding behavior of the DNA i-motif of the human telomere, dC₁₉, and a high-stability i-motif-forming sequence in the promoter of the human DNA repair gene RAD17 using human physiological solution and temperature conditions. We developed a circular-dichroism-spectroscopy-based pH titration method that is followed by analysis of titration curves in the derivative domain and found that the observed pH-dependent folding behavior can be significantly different and, in some cases, multiphasic, with a dependence on how rapidly i-motif folding is induced. Interestingly, the human telomere sequence exhibits unusual isothermal hysteresis in which the unfolding process always occurs at a higher pH than the folding process. For the RAD17 i-motif, rapid folding by injection into a low-pH solution results in triphasic unfolding behavior that is completely diminished when samples are slowly folded in a stepwise manner via pH titration. Chemical footprinting of the RAD17 sequence and pH titrations of dT-substituted mutants of the RAD17 sequence were used to develop a model of RAD17 folding and unfolding. These results may provide valuable information pertinent to i-motif use in sensors and materials, as well as insight into the potential biological activity of i-motif-forming sequences under stepwise or instantaneous changes in pH.