PHOTOINACTIVATION OF CATALASE OCCURS UNDER BOTH HIGH-TEMPERATURE AND LOW-TEMPERATURE STRESS CONDITIONS AND ACCOMPANIES PHOTOINHIBITION OF PHOTOSYSTEM-II

Severe photoinactivation of catalase (EC 1.11.1.6) and a decline of variable fluorescence (F(v)), indicating photoinhibition of photosynthesis, were observed as rapid and specific symptoms in leaves exposed to a high heat-shock temperature of 40-degrees-C as well as in leaves exposed to low chilling temperatures in white light of only moderately high photosynthetic photon flux density of 520 muE m-2 s-1. Other parameters, such as peroxidase (EC 1.11.1.7), glycolate oxidase (EC 1.1.3.1), glutathione reductase (EC 1.6.4.2), or the chlorophyll content, were hardly affected under these conditions. At a compatible temperature of 22-degrees-C, the applied light intensity did not induce severe photoinactivations. In darkness, exposures to high or low temperatures did not affect catalase levels. Also, decline of F(v) in light was not related to temperature sensitivity in darkness. The effective low-temperature ranges inducing photoinactivation of catalase differed significantly for chilling-tolerant and chilling-sensitive plants. In leaves of rye (Secale cereale L.) and pea (Pisum sativum L.), photoinactivation occurred only below 15-degrees-C, whereas inactivation occurred at 15-degrees-C in cucumber (Cucumis sativus L.) and maize (Zea mays L.). The behavior of F(v) was similar, but the difference between chilling-sensitive and chilling-tolerant plants was less striking. Whereas the catalase polypeptide, although photoinactivated, was not cleaved at 0 to 4-degrees-C, the D1 protein of photosystem II was greatly degraded during the low-temperature treatment of rye leaves in light. Rye leaves did not exhibit symptoms of any major general photodamage, even when they were totally depleted of catalase after photoinactivation at 0 to 4-degrees-C, and catalase recovered rapidly at normal temperature. In cucumber leaves, the decline of catalase after exposures to bright light at 0 to 4-degrees-C was accompanied by bleaching of chlorophyll, and the recovery observed at 25-degrees-C was slow and required several days. Similar to the Dl protein of photosystem II, catalase differs greatly from other proteins by its inactivation and high turnover in light. Inasmuch as catalase and D1 protein levels depend on continuous repair synthesis, preferential and rapid declines are generally to be expected in light whenever translation is suppressed by stress actions, such as heat or chilling, and recovery will reflect the repair capacity of the plants.