Dynamics of intrinsically disordered proteins and their functional roles

在这里，我们用核磁共振和质谱仪研究了异染色质相关蛋白Chp1和Swi6以及组蛋白多聚体的动态结构。异染色质相关蛋白Chp1的色域(CD)具有新的RNA结合活性和组蛋白H3K9me3结合活性。核磁共振显示Chp1CD与组蛋白H3K9me3结合的N端外区存在一个小螺旋。CenRNA的加入导致了Chp1CD中该螺旋和C末端螺旋中残基的酰胺质子的化学位移变化。此外，我们还揭示了H_2A/H_2B及其与组蛋白伴侣蛋白NAP1的C端无序酸性结构域的络合物的溶液结构。

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.