Isolation and characterization of a plant cDNA showing homology to animal glutathione peroxidases.
A cDNA library from freshly isolated protoplasts was differentially screened using cDNAs from mesophyll cells, stressed leaf strips and cell suspension cultures. One of the selected clones, 6P229, turned out to encode a putative polypeptide showing homology to the btuE periplasmic protein of Escherichia coli and to animal selenium-dependent glutathione peroxidases. A major difference was that the putative selenocysteine in the active site was not encoded by the termination codon TGA. The 6P229 gene was found to be expressed in germinating seeds, in apex and in flowers, as well as in stressed tissues. This pattern of expression would be consistent with a key role in cellular metabolism such as defense against oxidative stresses.
Criqui
M C
MC
Institut de Biologie Moléculaire des Plantes du C.N.R.S., Strasbourg, France.
Jamet
E
E
Parmentier
Y
Y
Marbach
J
J
Durr
A
A
Fleck
J
J
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics; D005979:Glutathione Peroxidase / Q000235:genetics*; D006801:Humans; D008969:Molecular Sequence Data; D010944:Plants / Q000201:enzymology / Q000235:genetics*; D015183:Restriction Mapping; D012689:Sequence Homology, Nucleic Acid
D005979:Glutathione Peroxidase