No abstract

a b s t r a c tHerbivore outbreaks, a major form of natural disturbance in many ecosystems, often have devastating impacts on their food plants. Understanding those factors permitting herbivore outbreaks to occur is a long-standing issue in conventional studies of plant-herbivore interactions. These studies are largely concerned with the relative importance of intrinsic biological factors and extrinsic environmental variations in determining the degree of herbivore outbreaks. In this paper, we illustrated that how the time delay associated with plant defense responses to herbivore attacks and the spatial diffusion of herbivore jointly promote outbreaks of herbivore population. Using a reaction-diffusion model, we showed that there exists a threshold of time delay in plant-herbivore interactions; when time delay is below the threshold value, there is no herbivore outbreak. However, when time delay is above the threshold value, periodic outbreak of herbivore emerges. Furthermore, the results confirm that during the outbreak period, plants display much lower density than its normal level but higher in the inter-outbreak periods. Our results are supported by empirical findings.Crown

No abstract

SummaryPlant adaptation in variable soil nitrate concentrations involves sophisticated signaling and transport systems that modulate a variety of physiological and developmental responses. However, we know very little about their molecular mechanisms. It has recently been reported that many of these responses are regulated by a transceptor NRT1.1, a transporter cum receptor of nitrate signaling. NRT1.1 displays dual-affinity modes of nitrate binding and establishes phosphorylated/non-phosphorylated states at the amino acid residue threonine 101 in response to fluctuating nitrate concentrations. Here we report that intrinsic structural asymmetries between the protomers of the homodimer NRT1.1 provide a functional basis for having dual-affinity modes of nitrate binding and play a pivotal role for the phosphorylation switch. Nitrate-triggered local conformational changes facilitate allosteric communications between the nitrate binding and the phosphorylation site in one protomer, but such communications are impeded in the other. Structural analysis therefore suggests the functional relevance of NRT1.1 interprotomer asymmetries.