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-Structure paper
タイトル | Structural basis of Ty3 retrotransposon integration at RNA Polymerase III-transcribed genes. |
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ジャーナル・号・ページ | Nat Commun, Vol. 12, Issue 1, Page 6992, Year 2021 |
掲載日 | 2021年11月30日 |
![]() | Guillermo Abascal-Palacios / Laura Jochem / Carlos Pla-Prats / Fabienne Beuron / Alessandro Vannini / ![]() ![]() ![]() |
PubMed 要旨 | Retrotransposons are endogenous elements that have the ability to mobilise their DNA between different locations in the host genome. The Ty3 retrotransposon integrates with an exquisite specificity ...Retrotransposons are endogenous elements that have the ability to mobilise their DNA between different locations in the host genome. The Ty3 retrotransposon integrates with an exquisite specificity in a narrow window upstream of RNA Polymerase (Pol) III-transcribed genes, representing a paradigm for harmless targeted integration. Here we present the cryo-EM reconstruction at 4.0 Å of an active Ty3 strand transfer complex bound to TFIIIB transcription factor and a tRNA gene. The structure unravels the molecular mechanisms underlying Ty3 targeting specificity at Pol III-transcribed genes and sheds light into the architecture of retrotransposon machinery during integration. Ty3 intasome contacts a region of TBP, a subunit of TFIIIB, which is blocked by NC2 transcription regulator in RNA Pol II-transcribed genes. A newly-identified chromodomain on Ty3 integrase interacts with TFIIIB and the tRNA gene, defining with extreme precision the integration site position. |
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手法 | EM (単粒子) |
解像度 | 3.98 Å |
構造データ | EMDB-13831, PDB-7q5b: |
由来 |
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![]() | DNA BINDING PROTEIN / Transcription / RNA Pol III / Ty3 Retrotransposon / Intasome |