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

Abstract

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 beta polypeptide sequence of 20. 19kd . Compared to other legume storage proteins, the alpha and beta 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.

The structure of rice storage protein glutelin precursor deduced from cDNA

“…Rice glutelin shares several characters in common with leguminous 11 S globulin. When the deduced amino acid sequence of the glutelin precursor was compared with those of pea legumin [5] and soybean glycinin [a], it showed 38 and 37% homology to them. The sequence of the acidic subunit is less conserved than that of the basic subunit.…”

“…In this paper, the nucleotide sequence of glutelin cDNA was determined, from which the complete amino acid sequence of the glutelin precursor was deduced. When compared with the amino acid sequences of pea legumin [5] and soybean glycinin [6], we found that rice glutelin shows homology to these leguminous 11 S globulins. This is the first complete nucleotide sequence of the rice storage protein gene.…”

A complete cDNA coding for the sequence of glycinin A2B1a subunit precursor

“…In these alternating patterns, the sequence spanning residues 244-254 of the A2Bra subunit precursor shows a relatively striking hydrophilicity, suggesting that it may be localized near the surface of the protein molecule. Although these hydrophilic sequences contained repeated units in glycinin A3B4 [S] and legumin cup [9,18], there are none in the A2Bra subunit precursor. However, these hydrophilic regions which are located immediately upstream of the post-translational cleavage sites of glycinin and legumin precursors appear to be functionally similar.…”

Molecular Cloning of a Novel Glutelin cDNA from Rice Seeds.

“…Rice glutelins share amino acid sequence homology with the 11S globulins of legume species, such as soybean glycinin [1] and pea legumin [2], but differ from other globulins in their insolubility in saline solutions. The glutelins are synthesized as preproglutelin (ca.…”