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J. Biol. Chem., Vol. 261, Issue 31, 14576-14581, 11, 1986

Structure of the rapeseed 1.7 S storage protein, napin, and its precursor

ML Ericson, J Rodin, M Lenman, K Glimelius, LG Josefsson and L Rask

Napin (1.7 S protein) is a basic, low molecular weight storage protein synthesized in rapeseed (Brassica napus) embryos during seed development. Napin is composed of two polypeptide chains with molecular weights of 9000 and 4000 that are held together by disulfide bonds. Comparison of the deduced amino acid sequence of a napin cDNA clone with that of napin peptide fragments established that napin is initially synthesized as a precursor of 178 residues. This polypeptide is subsequently processed through several proteolytic events, which ultimately generate the two mature napin chains, of 86 and 29 residues, respectively. Protein biosynthesis in vitro showed that the initial translation product (Mr 20,000) contains a signal sequence which is removed during transfer of the protein into the endoplasmic reticulum. Two additional peptides, of 22 and 19 residues, as well as the COOH- terminal residue, are also removed during maturation of napin, as deduced from the sequence comparison. Comparisons of the napin sequence with other known protein sequences established that there is a significant homology between napin and two other small seed proteins, the castor bean storage protein and a trypsin inhibitor from barley.
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