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Nucleic Acids Research, 1984, Vol. 12, No. 11 4493-4506
© 1984

MOLECULAR BIOLOGY

The complete nucleotide sequence of a legumin gene from pea (Pisum sativum L.)

Grantley W. Lycett*, Ronald R.D. Croy, Anil H. Shirsat and Donald Boulter

Department of Botany, University of Durham South Road, Durham DH1 3LE, UK

*To whom correspondence should be addressed

Received March 1, 1984. Revised May 2, 1984. Accepted May 2, 1984.

One of several genes coding for the major pea storage protein, legumin, has been completely sequenced. The sequence covers the whole of the transcribed region, plus 5' and 3' untranscribed sequences. The predicted protein sequence starts with a signal peptide and is followed by the legumin {alpha} polypeptide sequence of 36.44kd and the ß polypeptide sequence of 20.19kd. Compared to other legume storage proteins, the {alpha} and ß polypeptide sequences encoded by this legumin gene, which contain 3 met and 5 cys residues, are relatively rich in the sulphur amino acids. The coding sequence is interrupted by three introns which show boundary sequences typical of higher plant genes. The 5' end of the gene sequence contains a ‘TATA box’, a ‘CAAT box’ and a sequence showing some homology to an ‘AGGA box’. An extra sequence, identical to the normal polyadenylation signal of the legumin message is seen in the 3' untranscribed region. The structure of the gene and the possible significance of secondary structures in the nascent RNA transcript in affecting the choice of polyadenylation site is discussed.


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