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SNP haplotypes of the BADH1 gene and their association with aroma in rice (Oryza sativa L.)

Singh, Anuradha, Singh, Pradeep K., Singh, Rakesh, Pandit, Awadhesh, Mahato, Ajay K., Gupta, Deepak K., Tyagi, Kuldeep, Singh, Ashok K., Singh, Nagendra K., Sharma, Tilak R.
Molecular breeding 2010 v.26 no.2 pp. 325-338
Oryza sativa, alleles, amino acids, betaine, betaine-aldehyde dehydrogenase, binding capacity, breeding, chromosomes, cultivars, exons, genotyping, haplotypes, introns, landraces, models, odor compounds, odors, osmotolerance, population structure, rice, salt tolerance, single nucleotide polymorphism, water stress
Betaine aldehyde dehydrogenase (BADH) is a key enzyme involved in the synthesis of glycinebetaine—a powerful osmoprotectant against salt and drought stress in a large number of species. Rice is not known to accumulate glycinebetaine but it has two functional genes coding for the BADH enzyme. A non-functional allele of the BADH2 gene located on chromosome 8 is a major factor associated with rice aroma. However, similar information is not available regarding the BADH1 gene located on chromosome 4 despite the similar biochemical function of the two genes. Here we report on the discovery and validation of SNPs in the BADH1 gene by re-sequencing of diverse rice varieties differing in aroma and salt tolerance. There were 17 SNPs in introns with an average density of one per 171 bp, but only three SNPs in exons at a density of one per 505 bp. Each of the three exonic SNPs led to changes in amino acids with functional significance. Multiplex SNP assays were used for genotyping of 127 diverse rice varieties and landraces. In total 15 SNP haplotypes were identified but only four of these, corresponding to two protein haplotypes, were common, representing more than 85% of the cultivars. Determination of population structure using 54 random SNPs classified the varieties into two groups broadly corresponding to indica and japonica cultivar groups, aromatic varieties clustering with the japonica group. There was no association between salt tolerance and the common BADH1 haplotypes, but aromatic varieties showed specific association with a BADH1 protein haplotype (PH2) having lysine₁₄₄ to asparagine₁₄₄ and lysine₃₄₅ to glutamine₃₄₅ substitutions. Protein modeling and ligand docking studies show that these two substitutions lead to reduction in the substrate binding capacity of the BADH1 enzyme towards gamma-aminobutyraldehyde (GABald), which is a precursor of the major aroma compound 2-acetyl-1-pyrroline (2-AP). This association requires further validation in segregating populations for potential utilization in the rice breeding programs.