ABSTRACT
A system consisting of a flow-through chamber connected to a commercial infrared gas analysis system was developed to measure homopteran respiration during feeding. Using this system, respiration rates of 202 and 206 µmol CO(2) h(-1) g(-1) (4.96 and 5.04 ml CO(2) h(-1) g(-1)) were determined for whiteflies and cotton aphids, respectively, at 25 degrees C on diets containing 15% sucrose. These rates were considerably higher than those of other stationary insects, indicating that whiteflies and aphids maintain a relatively high metabolic rate when feeding. Whitefly respiration increased with temperature from 25 to 46 degrees C with a Q(10) of about 2 on diets containing 10, 15 and 20% sucrose, but less than 2 on diets containing 2.5 and 5% sucrose. Respiration rates were similar on the diets containing >10% sucrose, but were generally lower on the diets containing <10% sucrose. Respiration rates decreased upon extended exposure to 47 degrees C; the rate of decrease was inversely related to the dietary sucrose concentration up to 15%. The results indicate that whiteflies require a sucrose concentration of between 5 and 10% (i.e. 0.15 and 0.3 M) for maximum rates of metabolism while feeding. Higher concentrations of sucrose in the diet delayed high-temperature mortality, possibly a reflection of the high sucrose requirement for sorbitol synthesis in whiteflies.
ABSTRACT
We tested the hypothesis that light activation of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) is inhibited by moderately elevated temperature through an effect on Rubisco activase. When cotton (Gossypium hirsutum L.) or wheat (Triticum aestivum L.) leaf tissue was exposed to increasing temperatures in the light, activation of Rubisco was inhibited above 35 and 30 degreesC, respectively, and the relative inhibition was greater for wheat than for cotton. The temperature-induced inhibition of Rubisco activation was fully reversible at temperatures below 40 degreesC. In contrast to activation state, total Rubisco activity was not affected by temperatures as high as 45 degreesC. Nonphotochemical fluorescence quenching increased at temperatures that inhibited Rubisco activation, consistent with inhibition of Calvin cycle activity. Initial and maximal chlorophyll fluorescence were not significantly altered until temperatures exceeded 40 degreesC. Thus, electron transport, as measured by Chl fluorescence, appeared to be more stable to moderately elevated temperatures than Rubisco activation. Western-blot analysis revealed the formation of high-molecular-weight aggregates of activase at temperatures above 40 degreesC for both wheat and cotton when inhibition of Rubisco activation was irreversible. Physical perturbation of other soluble stromal enzymes, including Rubisco, phosphoribulokinase, and glutamine synthetase, was not detected at the elevated temperatures. Our evidence indicates that moderately elevated temperatures inhibit light activation of Rubisco via a direct effect on Rubisco activase.
