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. 2018 Sep 21;30(10):2352–2367. doi: 10.1105/tpc.18.00653

Figure 1.

Figure 1.

Yeast Two-Hybrid Assay of Interactions between OsELF3 and HAF1.

(A) Interaction analysis of OsELF3 (as bait) with prey constructs containing HAF1 truncated fragments.

(B) Interaction analysis between a series of truncated OsELF3 and HAF1 fragments. HAF1 fragments (amino acids 99–619 or 288–667) interact most strongly with the C-terminal domain of OsELF3 (amino acids 503–760).

(C) The substitution of leucine to serine (L558S) in OsELF3 abolishes its interaction with HAF1.

(D) The C-terminal domain of OsELF3 (amino acids 503–760) is essential for its homodimer formation. Empty pGBK (bait) and pGAD (prey) were used as negative controls. Blue clones in the X-Gal assay and clones that grow on QDO medium indicate protein interactions in the yeast cells. QDO indicates SD-Trp-Leu-His-Ade medium.