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Instruments / Technical Area	Publication Details	Published	Actions
I03-Macromolecular Crystallography	Structure of KAP1 tripartite motif identifies molecular interfaces required for retroelement silencing Guido A. Stoll , Shun-Ichiro Oda , Zheng-Shan Chong , Minmin Yu , Stephen H. Mclaughlin , Yorgo Modis Proceedings Of The National Academy Of Sciences 60 DOI: 10.1073/pnas.1901318116 Diamond Proposal Number(s): [15916] Open Access Show Abstract ▼ Abstract: Retroviruses can integrate their DNA into the host-cell genome. Inherited retroviral DNA and other transposable elements account for more than half of the human genome. Transposable elements must be tightly regulated to restrict their proliferation and prevent toxic gene expression. KAP1/TRIM28 is an essential regulator of transposable element transcription. We determined the crystal structure of the KAP1 TRIM. The structure identifies a protein–protein interaction site required for recruitment of KAP1 to transposable elements. An epigenetic gene silencing assay confirms the importance of this site for KAP1-dependent silencing. We also show that KAP1 self-assembles in solution, but this self-assembly is not required for silencing. Our work provides insights into KAP1-dependent silencing and tools for expanding our mechanistic understanding of this process.	Jul 2019

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