Overcoming drought-induced decreases in soybean leaf photosynthesis by measuring with CO2-enriched air.

Soybean [Glycine max (L.) Merr. cv. Williams 82 and A3127] plants were grown in the field under long-term soil moisture deficit and irrigation to determine the effects of severe drought stress on the photosynthetic capacity of soybean leaves. Afternoon leaf water potentials, stomatal conductances, intercellular CO2 concentrations and CO2-assimilation rates for the two soil moisture treatments were compared during the pod elongation and seed enlargement stages of crop development. Leaf CO2-assimilation rates were measured with either ambient (340 µl CO2 l(-1)) or CO2-enriched (1800 µl CO2 l(-1)) air. Although seed yield and leaf area per plant were decreased an average of 48 and 31%, respectively, as a result of drought stress, leaf water potentials were reduced only an average of 0.27 MPa during the sampling period. Afternoon leaf CO2-assimilation rates measured with ambient air were decreased an average of 56 and 49% by soil moisture deficit for Williams 82 and A3127, respectively. The reductions in leaf photosynthesis of both cultivars were associated with similar decreases in leaf stomatal conductance and with small increases in leaf intercellular CO2 concentration. When the CO2-enriched air was used, similar afternoon leaf CO2-assimilation rates were found between the soil moisture treatments at each stage of crop development. These results suggest that photosynthetic capacity of soybean leaves is not reduced by severe soil moisture deficit when a stress develops gradually under field conditions.

Regulation of coupling factor in field-grown sunflower: A Redox model relating coupling factor activity to the activities of other thioredoxin-dependent chloroplast enzymes.

Simultaneous, non-invasive measurements were made of the rate of photosynthetic CO2 fixation and the state of activation of the chloroplast CF1CF0-ATP synthase (CF) in field-grown sunflower (Helianthus annuus L.) during the dark-to-light transition at sunrise. CO2 fixation showed a linear response with light intensity from zero to about 500-700 µE m(-2) s(-1). However, at light intensities of only 5-22 µE m(-2) s(-1), the energetic threshold for activation of the CF was found to be significantly lowered (as compared to the pre-dawn state), presumably through reduction of the regulatory sulfhdryl groups of the γ-subunit of the CF. When these studies were extended to chamber-grown plants, it was found that as little as 5 seconds of illumination at 4 µE m(-2) s(-1) caused apparently full CF reduction. It is clear, therefore, that the catalytic activation of CF is not rate limiting to the induction of carbon assimilation under field conditions during a natural dark-to-light transition at sunrise. A model, based on the redox properties of the regulatory sulfhydryls, was developed to examine the significance of sulfhydryl midpoint potential in explaining the differences in light sensitivity and oxidation and reduction kinetics, between the CF and other thioredoxin-modulated chloroplast enzymes. Computer simulations of the light-induced regulation of three representative thioredoxin-modulated enzymes are presented.

Interaction of heat and salt shock in cultured tobacco cells.

Cultured tobacco cells (Nicotiana tabacum L. var Wisconsin-38) developed tolerance to otherwise nonpermissive 54 degrees C treatment when heat-shocked at 38 degrees C (2 h) but not at 42 degrees C. Heat-shocked cells (38 degrees C) exhibited little normal growth when the 54 degrees C stress came immediately after heat shock and normal growth when 54 degrees C stress was administered 8 hours after heat shock. Heat shock extended the length of time that the cells tolerated 54 degrees C. Tobacco cells developed tolerance to otherwise lethal 2% NaCl treatment when salt-shocked (1.2% NaCl for 3 hours). The time course for salt tolerance development was similar to that of thermotolerance. Heat-shocked cells (38 degrees C) developed tolerance of nonpermissive salt stress 8 hours after heat shock. Alternatively, cells heat-shocked at 42 degrees C exhibited immediate tolerance to lethal salt stress followed by a decline over 8 hours. Radioactive methionine incorporation studies demonstrated synthesis of heat shock proteins at 38 degrees C. The apparent molecular weights range from 15 to 115 kilodaltons with a protein complex in the 15 to 20 kilodalton range. Synthesis of heat shock proteins appeared to persist at 42 degrees C but with large decreases in incorporation into selected heat shock protein. During salt shock, the synthesis of normal control proteins was reduced and a group of salt shock proteins appeared 3 to 6 h after shock. Similarities between the physiology and salt shock proteins/heat shock proteins suggest that both forms of stress may share common elements.