Characterization of y-type high-molecular-weight glutenins in tetraploid species of Leymus.

Three y-type high-molecular-weight (HMW) glutenin gene open reading frames (ORFs), Chiy1, Chiy2, and Racy, were isolated and characterized from Leymus chinensis PI499516 and Leymus racemosus ssp. racemosus W623305. They shared an extra glutamine in the N-terminal and LAAQLPAMCRL peptides in the C-terminal with x-type HMW glutenins but had different N-terminal lengths. Like other y-type HMW glutenins, Chiy2 and Racy had 104 (or 105) amino acid (aa) residues at the N-terminal and started with EGEASR, whereas Chiy1 had 99 aa in this domain and started with QLQCER because of the deletion of EGEASR. Five other y-type glutenins, including those from Elymus ciliaris, Pseudoroegneria libanotica, and Leymus mollis, were similar to Chiy1. The ORF of Chiy2 was probably not expressed. The ORFs of both Chiy1 and Racy were expressed in bacteria. The maximum likelihood phylogenic tree based on the signal peptide and N-terminal and C-terminal aa residues revealed two clades of y-type HMW glutenins in Triticeae; the first contained Ay, By, Cy, Dy, Eey, Gy, Ky, Ry, Tay, and Uy, while the second clade contained the remaining y types, including those from Leymus. Within the second clade, HMW glutenins lacking the EGEASR peptide formed a subclade. These y-type HMW glutenins in Leymus could not be targeted to the Xm or Ns genome.