PAG-IX: ISOLATION OF 1AX2*B A NEW MUTANT HMW GLUTENIN SUBUNIT GENE IN COMMON WHEAT (TRITICUM AESTIVUM L.)

PAG-IX   Plant & Animal Genome IX Conference

Town & Country Hotel, San Diego, CA, January 13-17, 2001.


Poster: Sequencing & EST
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ISOLATION OF 1AX2*B A NEW MUTANT HMW GLUTENIN SUBUNIT GENE IN COMMON WHEAT (TRITICUM AESTIVUM L.)

ANGÉLA JUHÉSZ1, LÁSZLÓ TAMÁS2, ILDIKÓ KARSAI1, GYULA VIDA1, LÁSZLÓ LÁNG1, ZOLTÁN BEDÕ1

1 Agricultural Research Institute of the Hungarian Academy of Sciences, Brunszvik u. 2, Martonvásár, 2462, Hungary
2 Department of Plant Physiology of the Loránd Eõtvõs University, Múzeum u. 3, Budapest, 1088, Hungary

In our research programme we studied HMW glutenin subunit composition of an old Hungarian wheat variety, Bánkúti 1201. This variety has a genetically heterogeneous population consisting of lines with different storage protein compositions. When the population was divided into lines on the basis of HMW glutenin subunit composition a fragment measuring approx. 1300 bp characteristic of Bþnkîti 1201 was identified using HMW gene specific primers. Sequencing was carried out on clones which contain the 1300 bp fragment. Compared the results with the sequences of the 1Ax type HMW glutenin genes in the data base, the 1300 bp fragment showed almost 100% similarity with the relevant section of the 1Ax2* gene. Despite the homologyb the 1300 bp product was not present in the control varieties and genotypes containing the 1Ax2* HMW gutenin subunit. The computer analysis of the sequences confirmed that the gene containing the 1300 bp fragment is a mutation of 1Ax2*, designated as 1Ax2*B. The only difference was at the 1181 bp point of the coding region of gene 1Ax2* there was a C-G point mutation. The point mutation also influenced the derived amino acid sequence, resulting in a serine to cysteine change. The extra cysteine showed a positive influence on the functional properties. The results underline the importance of old landraces and varieties as valuable gene sources for plant breeding.


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