IndraLab

Statements

USP39 binds H2AB. 6 / 6
| 6
reach
"Isothermal titration calorimetry (ITC) assays further confirmed that Sad1 bound H2AB and H2AZB with comparable dissociation constants (K ) of 9.5 μM and 7.5 μM, respectively (Fig. 1c), indicating that Sad1 does not have a binding preference for H2A or H2A.Z."
38773107
reach
"To reveal the structural basis of the interaction between Sad1 and H2AB, we first dissected the structural elements of Sad1 required for the Sad1-H2AB interaction."
38773107
reach
"The binding between Sad1 and H2AB is mediated by electrostatic and hydrophobic interactions (Figs."
38773107
reach
"The Sad1 F118A mutation destabilized the Sad1-H2AB complex, and the substitution of Sad1 F118 with a positively charged arginine residue (F118R) severely diminished the interaction between Sad1 and H2AB (Fig. 2d)."
38773107
reach
"In addition, charge-reverse mutations of D114 and E117 decreased binding affinity between Sad1 and H2AB by 5.6-fold (Fig. 2d)."
38773107
reach
"By screening some known silencing factors, our in vitro pull-down assays identified that Clr3 and Sir2 directly interact with the Sad1-H2AB complex (Figs."
38773107