Photoinactivation of Catalase Occurs under Both High- and Low-Temperature Stress Conditions and Accompanies Photoinhibition of Photosystem II

Abstract

Severe photoinactivation of catalase (EC 1.11.1.6) and a decline of variable fluorescence (FJ), indicating photoinhibition of photosynthesis, were observed as rapid and specific symptoms in leaves exposed to a high heat-shock temperature of 40°C as well as in leaves exposed to low chilling temperatures in white light of only moderately high photosynthetic photon flux density of 520 ME m-2 s-'. 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°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, 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°C, whereas inactivation occurred at 15°C in cucumber (Cucumis sativus L.) and maize (Zea mays L.). The behavior of F, was similar, but the difference between chilling-sensitive and chillingtolerant plants was less striking. Whereas the catalase polypeptide, although photoinactivated, was not cleaved at 0 to 4°C, the Dl protein of photosystem 11 was greatly degraded during the lowtemperature 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°C, and catalase recovered rapidly at normal temperature. In cucumber leaves, the decline of catalase after exposures to bright light at 0 to 4°C was accompanied by bleaching of chlorophyll, and the recovery observed at 25°C was slow and required several days. Similar to the Dl protein of photosystem 11, catalase differs greatly from other proteins by its inactivation and high turnover in light. Inasmuch as catalase and Di 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.

Photosynthesis and antioxidant activity in Jatropha curcas L. under salt stress

“…This phenomenon was previously reported in purslane (Yazici et al, 2007), jatropha (Silva et al, 2010), rice (Lee et al, 2001), pea (Moran et al, 1994), bean (Jebara et al, 2005), and the mangrove Bruguiera parviflora (Parida et al, 2004). CAT deactivation by salt stress may be due to the prevention of new enzyme synthesis (Feierabend et al, 1992) or CAT photo-inactivation (Polle, 1997).…”

“…The activities of CAT were decreased at all concentrations of NaCl (Table 4), possibly due to the increase in H 2 O 2 levels, as seen in Table 3 (Lee et al, 2001). Feierabend et al (1992) have shown that under stress conditions inactivation of CAT is linked to H 2 O 2 accumulation. Loss of CAT activity due to salt stress in cotton (Gossett et al, 1994), sunflower (Santos et al, 2001), and rice (Lee et al, 2001), as well as due to photo-oxidative stress in tobacco chloroplasts (Miyagawa et al, 2000), is consistent with our results for J. curcas.…”

“…Loss of CAT activity due to salt stress in cotton (Gossett et al, 1994), sunflower (Santos et al, 2001), and rice (Lee et al, 2001), as well as due to photo-oxidative stress in tobacco chloroplasts (Miyagawa et al, 2000), is consistent with our results for J. curcas. The inhibition of CAT and APX activities by salt stress may be a consequence of downregulated gene expression or degradation, denaturation and/or inhibition/ inactivation of these proteins (Feierabend et al, 1992;Lee et al, 2001). Still, ongoing protein synthesis is required to maintain enzyme activity under conditions in which degradation exceeds re-synthesis and enzyme activity otherwise decreases (Cavalcanti et al, 2004).…”

Exogenous salicylic acid alleviates cold damage by regulating antioxidative system in two barley (Hordeum vulgareL.) cultivars

“…Therefore, our results suggest that the increase in the CAT activity in both cultivars can be a result of the scavenging of H 2 O 2 produced excessively in cell during cold stress, and CAT is an important H 2 O 2 scavenging enzyme leading to the cold tolerance of barley plants. However, certain research studies reported reduced CAT activity in plants exposed to low temperatures and bright light due to photo-inactivation of CAT (Feierabend et al 1992). In addition, it is concluded that exposure to cold temperatures causes an increase in CAT activity (Farooq et al 2008), which supports our results.…”

Light stress effects and antioxidative protection in two desert plants

“…In spite of the multitude of protective mechanisms, the peroxisomal enzyme catalase and the PSII reaction centre appear to exhibit a preferential light-sensitivity in leaves of most plants investigated so far (Feierabend, Schaan & Hertwig 1992;Aro, Virgin & Andersson 1993). The enzyme catalase is continuously inactivated by visible light in leaves but under non-stressed conditions the loss by photoinactivation can be compensated for by new synthesis.…”