2017 Fiscal Year Final Research Report
The structural study of heterochromatin by cryo-EM
Project/Area Number |
16K18473
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Research Category |
Grant-in-Aid for Young Scientists (B)
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Allocation Type | Multi-year Fund |
Research Field |
Genome biology
|
Research Institution | Waseda University |
Principal Investigator |
|
Project Period (FY) |
2016-04-01 – 2018-03-31
|
Keywords | エピジェネティクス / クロマチン / ヒストン / ヘテロクロマチン / HP1 / ヒストン修飾 |
Outline of Final Research Achievements |
Heterochromatin functions as an important component for gene silencing and genome maintenance by the formation of condensed chromatin structures. The methylation of histone H3 at lysine 9 (H3K9me3) and its recognition by HP1 represent heterochromatin formation. However, it is unclear how HP1 folds chromatin containing H3K9me3 into condensed chromatin. In this study, we reconstituted H3K9me3 chromatin complexed with human HP1, and determined the structure of H3K9me3 chromatin complexed with HP1 by cryogenic electron microscopy.
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Free Research Field |
構造生物学
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