Identification of a new class of recombinant prolamin genes in wheat

Ila J. Nagy, Imre Takács, Angéla Juhász, László Tamás, Zoltán Bedo

Research output: Contribution to journalArticle

14 Citations (Scopus)


A novel storage protein gene with obvious wheat chimeric structure was isolated from an immature kernel-specific cDNA library prepared from the old Hungarian variety, Bánkúti 1201. This clone contains γ-gliadin sequences in the 5′ region and LMW-glutenin sequences on the 3′ end. A frameshift mutation was also introduced by the putative recombination event. Hence, the amino acid sequence of the C-terminal region was transformed to a completely new polypeptide. Based on this finding, 7 additional recombinant prolamin genes of similar structure were isolated with specific PCR primers. The 8 chimeric clones seem to be derived from 4 individual γ-gliadin and 3 LMW-glutenin sequences. These genes show remarkable diversity in size, gliadin:glutenin ratio, frameshift mutations, and sulphur content. The putative functional characteristics of the chimeric polypeptides and problems related to the origin of the encoding genes are discussed.

Original languageEnglish
Pages (from-to)840-847
Number of pages8
Issue number5
Publication statusPublished - Oct 2005


  • Chimeric genes
  • Prolamin
  • Recombination
  • Wheat cDNA library

ASJC Scopus subject areas

  • Biotechnology
  • Molecular Biology
  • Genetics

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