Characterisation of a full-length cDNA clone for pea ferredoxin-NADP+ reductase

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Abstract
Ferredoxin-NADP+ reductase has been purified to homogeneity from pea leaves and has been resolved into two forms by ion exchange chromatography and SDS gel electrophoresis. Antibodies to the proteins have been used to isolate pea leaf cDNA clones from a library in λgt11. A full-length clone of 1 400 bp encodes a polypeptide of 360 amino acid residues, of which 52 residues constitute an N-terminal transit peptide and 308 residues make up the mature protein. Transcription and translation of the cDNA in vitro produces a protein of 40 kDa, which is imported by isolated pea chloroplasts and processed to the mature 34 kDa protein. Southern hybridisation to pea genomic DNA indicates that there are probably two genes in the haploid genome.