| Budget Amount *help |
¥124,800,000 (Direct Cost: ¥96,000,000、Indirect Cost: ¥28,800,000)
Fiscal Year 2012: ¥31,200,000 (Direct Cost: ¥24,000,000、Indirect Cost: ¥7,200,000)
Fiscal Year 2011: ¥31,200,000 (Direct Cost: ¥24,000,000、Indirect Cost: ¥7,200,000)
Fiscal Year 2010: ¥31,200,000 (Direct Cost: ¥24,000,000、Indirect Cost: ¥7,200,000)
Fiscal Year 2009: ¥31,200,000 (Direct Cost: ¥24,000,000、Indirect Cost: ¥7,200,000)
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| Research Abstract |
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.
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