IndraLab

Statements

Histone binds USP39. 9 / 9
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"These results indicate that the interaction between Sad1 and histones is required for the distribution of Sad1 in the nuclear envelope but not for its localization to the SPB."
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"We next investigated whether the interaction between Sad1 and histones is important for the centromere-NE association."
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"These data indicate that the interaction between Sad1 and histone is not involved in centromere clustering at SPB, which is consistent with the previous finding that Sad1 is essential for linking centromeres with SPB ."
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"To further examine whether histone could bind to the USP39 promoter active region in vitro, an EMSA was conducted."
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"These results indicated that histone indeed bound to the predicted promoter active region binding site of USP39 in vitro."
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"We hypothesize that these nuclear membrane proteins may form a synergistic network to create a microenvironment to benefit heterochromatin organization and maintenance at the nuclear periphery, which requires further investigation.Fission yeast Sad1 binds both canonical histone H2A-H2B and histone variant H2A.Z-H2B, whereas the budding yeast SUN-family protein, Mps3, specifically recognizes H2A.Z ."
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"These results indicated that histone indeed bound to the predicted promoter active region binding site of USP39 in vitro."
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"To examine the effect of 5 R mutation on the interaction between Sad1 and histone in vivo, we created a stain carrying Sad1-5R-HA and H2B -FLAG and conducted Co-IP experiments."
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"8b, c), indicating that Sad1 associates with heterochromatin regions.Next, we wanted to test whether the histone binding activity of Sad1 is important for heterochromatin silencing."
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