Abstract
A cDNA encoding the chloroplastic copper/zinc-superoxide dismutase of pea (Pisum sativum L.) was isolated from a cDNA library constructed in lambda gt11 from leaf mRNA. Nucleotide sequence analysis of the 875-base-pair clone revealed that it contained the complete coding sequence of the mature superoxide dismutase isozyme subunit, along with sequence information for a 48-amino acid N-terminal transit peptide. The deduced amino acid sequence of the mature subunit proved to be 64-87% homologous with amino acid sequences of copper/zinc-superoxide dismutases from other plant species. In vitro transcription, followed by cell-free translation, of the cDNA resulted in the formation of a 23.5-kDa precursor polypeptide, which, upon incubation with isolated pea chloroplasts, was imported and processed to its mature subunit molecular mass of 17.4 kDa.
MeSH Terms
Amino Acid Sequence
Base Sequence
Brassica
Chloroplasts/enzymology
Cloning, Molecular
DNA/genetics
DNA Restriction Enzymes
Electrophoresis, Polyacrylamide Gel
Fabaceae
Isoenzymes/genetics
Molecular Sequence Data
Plants/enzymology,genetics
Plants, Medicinal
Protein Biosynthesis
Superoxide Dismutase/genetics
Transcription, Genetic
Vegetables
Zea mays
Chemicals
Isoenzymes
DNA
Superoxide Dismutase
DNA Restriction Enzymes
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Scioli J R
Department of Biochemistry and Microbiology, Cook College, Rutgers University, New Brunswick, NJ 08903.
Zilinskas B A
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