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Abstract
A glycine to serine change in Puroindoline b is associated with wheat grain hardness and low levels of starch-surface Friabilin. Theoretical and Applied Genetics 95:857-864
Giroux,M.J. and Morris,C.F.
USDA/ARS Western Wheat Quality Lab
The quantitative level of friabilin 15-kDa protein present in the surface of water-washed starch is highly correlated with wheat grain softness. Friabilin is composed primarily, if not exclusively, of the proteins puroindoline a and b. The transcript levels of these two proteins are similar among hard and soft wheat varieties, and the expression of both is controlled by the short arm of chromosome 5D, also the chromosomal location of the Hardness gene. We report here a glycine to serine sequence change in puroindoline-b mutation, hard grain texture and low levels of starch surface friabilin lines derived from the soft-textured variety 'Chinese Spring' and the substitution line 'Chinese Spring' containing the 5D chromosome of the hard-textures variety 'Cheyenne'. The sequence change reported here may adversely affect the lipid-binding properties of puroindoline-b and so effect hard grain texture. The results from puroindoline-b functionality such that the Hardness gene is a direct manifestation of puroindoline structure. We are suggesting the tentative molecular structure. We are suggesting the tentative molecular marker loci designations of Pinb-D1a and Pinb-D1b for the glycine and serine puroindoline-b types, respectively.
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