IndraLab

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"The interaction between Sad1 and H2A-H2B was also held when the GST pull-down assay was performed using a single-chain fusion of H2A and H2B (hereafter referred to as H2AB) (Supplementary Fig. 1b), which has been shown to be structurally similar to the wild type H2A-H2B heterodimer ."

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"Our results revealed a nucleosome-independent function of H2A-H2B: H2A-H2B physically associates with Sad1 to regulate Sad1’s interaction with other factors, such as Sir2 and Clr3, and promote the LLPS ability of Sad1."

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"We solved the crystal structure of the histone binding motif (HBM) of Sad1 in a complex with a H2A-H2B fusion protein and showed that the DEF/Y motif of Sad1 binds H2A-H2B."