Characterization of a cDNA encoding CuZn-superoxide dismutase from the liverwort Marchantia paleacea var. diptera.

Suspension-cultured cells of the liverwort Marchantia paleacea var. diptera contain a cytosolic CuZn-superoxide dismutase (SOD) whose N-terminal amino acid sequence is similar to those of the isozymes found in chloroplasts of higher plants [Tanaka et al. (1996) Plant Cell Physiol. 37: 523]. A cDNA (MSODCc) encoding the cytosolic CuZn-SOD was isolated from cDNA library constructed from a liverwort cell suspension culture. The deduced amino acid sequence showed a higher degree of homology with the sequences of CuZn-SODs in chloroplasts than those in the cytosol of higher plants and an unique additional peptide in the C-terminal region, but no plastid transit sequence. Northern blotting using MSODCc as a probe and immunoblot analysis with antiserum against the enzyme revealed that the steady state level of transcript was not affected by copper, but both CuZn-SOD protein and its activity increased.