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"Thus, our mutagenesis analyzes supported the importance of hydrophobic and electrostatic interactions in coordinating the interaction between Sad1 and H2AB.Notably, the core histone-binding fragment of Sad1 contains a DEF/Y motif commonly identified in H2A-H2B or H2A.Z-H2B-binding proteins, including Chz1, Anp32e, Swr1, and the suppressor of Ty16 (Spt16) (Fig. 2e), and showed a conserved histone recognition mode (Supplementary Fig. 5)."