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Cloning and characterization of a cDNA encoding a sulfur-rich coixin

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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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Authors and Affiliations

  1. Centro de Biologia Molecular e Engenharia Genética, Universidade Estadual de Campinas, 13081, Campinas, SP, Brazil

    Adilson Leite, José Andrés Yunes, Silvia Regina Turcinelli & Paulo Arruda

  2. Departamento de Genética e Evolução, IB, Universidade Estadual de Campinas, 13081, Campinas, SP, Brazil

    Paulo Arruda

Authors
  1. Adilson Leite
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  2. José Andrés Yunes
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  3. Silvia Regina Turcinelli
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  4. Paulo Arruda
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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

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