Abstract
A full-length cDNA clone encoding a sulfur-richCoix prolamin was isolated using a cDNA library constructed from polysomal mRNA prepared from immatureCoix endosperm. The deduced amino acid sequence of the cDNA clone predicted a polypeptide of 194 residues, which shared 64% homology with the 17 kDa β-zein. The mature protein contains the familiar composition of the prolamins and an unusually high content of the sulfur-containing amino acids methionine (11.6%) and cysteine (5.2%).In vitro transcription followed byin vitro translation of the coding region of the pBCX17.9S clone gave rise to a polypeptide with an apparent molecular weight corresponding to the C4 α-coixin. Hydropathy analysis showed that C4 α-coixin is slightly more hydrophobic than β-zein.
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Leite, A., Yunes, J.A., Turcinelli, S.R. et al. Cloning and characterization of a cDNA encoding a sulfur-rich coixin. Plant Mol Biol 18, 171–174 (1992). https://doi.org/10.1007/BF00018475
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DOI: https://doi.org/10.1007/BF00018475