Cloning and characterization of a cDNA encoding the chloroplastic copper/zinc-superoxide dismutase from pea

A cDNA clone encoding the chloroplastic copper/zinc-superoxide dismutase of pea (Pisum sativum L.) was isolated from a cDNA library constructed in λ gt11 from leaf mRNA. Nucleotide sequence analysis of the 875-base-pair clone revealed that it contained the complete coding sequence of the mature supe...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1988-10, Vol.85 (20), p.7661-7665
Main Authors: Scioli, J.R, Zilinskas, B.A
Format: Article
Language:English
Subjects:
ACIDE AMINE
ADN
Amino Acid Sequence
AMINO ACIDS
AMINOACIDOS
ARN
Base Sequence
Biological and medical sciences
Brassica
Chloroplasts
Chloroplasts - enzymology
CLONACION
CLONAGE
CLONING
Cloning, Molecular
CODE GENETIQUE
CODIGO GENETICO
Complementary DNA
Corn
DNA
DNA - genetics
DNA Restriction Enzymes
Electrophoresis, Polyacrylamide Gel
ENZIMAS
ENZYME
ENZYMES
Fabaceae
Fundamental and applied biological sciences. Psychology
Gels
Genes. Genome
GENETIC CODE
Isoenzymes - genetics
Molecular and cellular biology
Molecular genetics
Molecular Sequence Data
NUCLEOTIDE
Nucleotide sequences
NUCLEOTIDES
NUCLEOTIDOS
Peas
PISUM SATIVUM
Plants
Plants - enzymology
Plants - genetics
Plants, Medicinal
PLASTE
PLASTIDIOS
PLASTIDS
Protein Biosynthesis
RNA
Superoxide Dismutase - genetics
Superoxides
Transcription, Genetic
Vegetables
Zea mays
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Description
Summary:A cDNA clone encoding the chloroplastic copper/zinc-superoxide dismutase of pea (Pisum sativum L.) was isolated from a cDNA library constructed in λ 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.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.85.20.7661