Abstract
A cDNA clone (pFD1) derived from Silene pratensis ferredoxin mRNA was selected from a cDNA-library using the hybrid released translation technique. Nucleotide sequence analysis showed the cDNA insert to contain the complete coding region of the ferredoxin precursor protein. The ferredoxin precursor has a mol.wt. of 15 300, the transit-peptide has a mol.wt. of 5600. The length of the ferredoxin mRNA was found to be 700 nucleotides whereas the cDNA insert was about 1200 basepairs. S1 nuclease protection experiments showed the ferredoxin-specific DNA to be 660 basepairs in length and to start 39 nucleotides upstream of the ferredoxin coding sequence. Southern blot analysis of genomic DNA revealed the presence of only one fragment with homology to the ferredoxin cDNA probe, so it is probably a single-copy gene. Comparison of the ferredoxin transit-sequence with transit sequences of another stromal protein, the small subunit of ribulosebisphosphate carboxylase showed no apparent homology, except for a stretch of three amino acids near the processing site.
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