Cloning and characterization of a cDNA encoding a sulfur-rich coixin.
A full-length cDNA clone encoding a sulfur-rich Coix prolamin was isolated using a cDNA library constructed from polysomal mRNA prepared from immature Coix endosperm. The deduced amino acid sequence of the cDNA clone predicted a polypeptide of 194 residues, which shared 64% homology with the 17 kDa beta-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 by in 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 alpha-coixin. Hydropathy analysis showed that C4 alpha-coixin is slightly more hydrophobic than beta-zein.
Leite
A
A
Centro de Biologia Molecular e Engenharia Genética, Universidade Estadual de Campinas, SP, Brazil.
Yunes
J A
JA
Turcinelli
S R
SR
Arruda
P
P
D000595:Amino Acid Sequence; D001483:Base Sequence; D003001:Cloning, Molecular; D008969:Molecular Sequence Data; D010940:Plant Proteins / Q000737:chemistry / Q000235:genetics*; D006109:Poaceae / Q000235:genetics*; D012689:Sequence Homology, Nucleic Acid; D015028:Zein / Q000737:chemistry
D010940:Plant Proteins; C072398:alpha-coixin protein, Coix lacryma-jobi; D015028:Zein