Dynamics of intrinsically disordered proteins and their functional roles

在这里，我们已经研究了动力学结构的内在无序的蛋白质，包括异染色质相关的蛋白质，Chp 1和Swi 6除了组蛋白多聚体通过NMR和MS。的chromodomain（CD）的异染色质相关的蛋白质，Chp 1，具有新的RNA结合活性，以及组蛋白H3 K9 me 3结合活性。NMR显示Chp 1 CD的N-末端外侧区域存在一个小螺旋，与组蛋白H3 K9 me 3结合。cenRNA的添加导致Chp 1 CD中该螺旋和C-末端螺旋内残基的酰胺质子的化学位移变化。此外，我们还揭示了H2 A/H2 B的溶液结构及其与组蛋白伴侣Nap 1的C-末端无序酸性结构域的复合物。

Here, we have examined dynamical structures of intrinsically disordered proteins including heterochromatin-related proteins, Chp1 and Swi6 in addition to histone multimers by NMR and MS. The chromodomain (CD) of a heterochromatin-related protein, Chp1, possesses novel RNA-binding activity as well as histone H3K9me3-binding activity. NMR revealed that the presence of a small helix in the N-terminal outside region of Chp1 CD bound to histone H3K9me3. Addition of cenRNA led to chemical shift changes of amide protons for residues within this helix and a C-terminal helix in Chp1 CD. In addition we revealed the solution structure of H2A/H2B and its complex with the C-terminal disordered acidic domain of histone chaperone Nap1.