In:
Genome, Canadian Science Publishing, Vol. 48, No. 5 ( 2005-10-01), p. 840-847
Abstract:
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.Key words: prolamin, chimeric genes, recombination, wheat cDNA library.
Type of Medium:
Online Resource
ISSN:
0831-2796
,
1480-3321
Language:
English
Publisher:
Canadian Science Publishing
Publication Date:
2005
detail.hit.zdb_id:
2020635-5
SSG:
12
