2016 Fiscal Year Final Research Report
Histone chaperone regulates higher order chromatin structure
| Project/Area Number |
26440001
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Multi-year Fund |
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| Section | 一般 |
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| Research Field |
Molecular biology
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| Research Institution | Hokkaido University |
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Principal Investigator |
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| Project Period (FY) |
2014-04-01 – 2017-03-31
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| Keywords | Pdr1 / FACT / HP1 / Spt16 / Pob3 / Swi6 / Histone / H3K9me |
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| Outline of Final Research Achievements |
Histone chaperones cooperatively function for chromatin structure regulation. In this project, we have clarified the mechanism of chromatin regulation by FACT complex. From proteomics analysis,Pdr1, HP1, and Fip1 were identified as FACT associating factors, and chromatin structural changes caused by conjugation with FACT were analyzed. As Pdr1 is a transcription factor that activates the xenobiotics elimination system, it became clear that this activator for the efflux pump system transiently evicts the nucleosome from the promoter chromatin, and reorganizes chromatin structure via FACT.
HP1 (Heterochromatin Protein 1) is known as a platform of heterochromatin forming factors. Our analysis revealed that it stabilizes the nucleosome octamer through the physical interaction with FACT complex at histone H3K9 methylated loci.
Fip1 analysis is currently underway. Our data related to chromatin silencing was obtained near the boundary of CnpA / H3 at the pericentromeric heterochromatin.
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| Free Research Field |
エピゲノム
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