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Shrestha, K 2011, 'Analysis of betaine aldehyde dehydrogenase encoding genes in wheat', MSc thesis, Southern Cross University, Lismore, NSW.

Copyright K Shrestha 2011


Betaine aldehyde dehydrogenase (BADH) is an important enzyme which has dual roles in cereals influencing abiotic stress tolerance and rice fragrance. Most grass species have two BADH paralogs (BADH1 and BADH2). A mutation in some BADH2 alleles introduces a termination codon which causes truncation of the protein and ultimately elevates the level of 2 acetyl-1-pyroline, leading to fragrance in rice and soybean. Bread wheat is hexaploid containing three genomes A, B and D. Identifying the potential number of BADH isozymes in wheat may indicate if it is possible to generate fragrant wheat by knocking out one, two or three homeologs. The hexaploid wheat variety Cadoux has three orthologs for both the BADH paralogs while its progenitors have a single ortholog. RT-PCR suggests only one homeolog of both BADH1 and BADH2 is expressed at two different time points (14 DPA and 30 DPA) in two different tissues (seeds and leaves) in hexaploid wheat variety Cadoux. Analysis of BADH1 and BADH2 gene expression in three other varieties in two different time points (14 DPA and 30 DPA) and two different tissues (seeds and leaves) also indicates that only the “A” genome homeolog is expressed. More research needs to undertaken to determine the exact function of this gene in wheat.