Mv. Rao et al., DIFFERENTIAL RESPONSE OF PHOTOSYNTHETIC PIGMENTS, RUBISCO ACTIVITY AND RUBISCO PROTEIN OF ARABIDOPSIS-THALIANA EXPOSED TO UVB AND OZONE, Photochemistry and photobiology, 62(4), 1995, pp. 727-735
The effect of UVB (280-320 nm radiation) and ozone (O-3) on growth, ph
otosynthetic pigments, ribulose bisphosphate carboxylase/oxygenase (ru
bisco) activity and rubisco protein were investigated in Arabidopsis t
haliana genotypes wild type Landsberg erecta (LER) and tt5, a flavonoi
d-deficient mutant. The UVB exposure for 5 days decreased whole plant
dry weight of only tt5 plants, while O-3 exposure decreased the whole
plant dry weight of both genotypes. The UVB exposure enhanced chloroph
ylls and carotenoids in both genotypes while O-3 exposure decreased ph
otosynthetic pigments in both genotypes. Both UVB and O-3 exposure enh
anced UV-absorbing compounds in LER but not in tt5. Ultraviolet-B expo
sure decreased initial and total rubisco activities only in tt5 plants
, which contained smaller amounts of UV-absorbing pigments. The effect
of UVB was greater on initial rubisco activity resulting in decreased
percent activatible rubisco. Ozone exposure decreased initial and tot
al rubisco activities in both genotypes, and the magnitudes of decreas
e were greater on total rubisco activity, resulting in enhanced levels
of percent activatible rubisco, Immunoblot analysis performed with an
tibodies raised against rubisco large subunit (LSU) and rubisco small
subunit (SSU)showed no major changes in the levels of rubisco protein
of either genotype irradiated with UVB. However, both rubisco LSU and
SSU decreased in tt5 plants exposed to UVB for 7 days (70% of total le
af area necrotic). In contrast, O-3 exposure of both the genotypes dec
reased the levels of rubisco LSU and SSU before the appearance of visi
ble symptoms of injury. These results suggested that UVB-induced limit
ations of growth are independent of changes in rubisco protein while O
-3-induced growth limitations appeared to be due to a significant redu
ction in rubisco protein.