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-Structure paper
タイトル | KAP1 is an antiparallel dimer with a functional asymmetry. |
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ジャーナル・号・ページ | Life Sci Alliance, Vol. 2, Issue 4, Year 2019 |
掲載日 | 2019年8月19日 |
著者 | Giulia Fonti / Maria J Marcaida / Louise C Bryan / Sylvain Träger / Alexandra S Kalantzi / Pierre-Yves Jl Helleboid / Davide Demurtas / Mark D Tully / Sergei Grudinin / Didier Trono / Beat Fierz / Matteo Dal Peraro / |
PubMed 要旨 | KAP1 (KRAB domain-associated protein 1) plays a fundamental role in regulating gene expression in mammalian cells by recruiting different transcription factors and altering the chromatin state. In ...KAP1 (KRAB domain-associated protein 1) plays a fundamental role in regulating gene expression in mammalian cells by recruiting different transcription factors and altering the chromatin state. In doing so, KAP1 acts both as a platform for macromolecular interactions and as an E3 small ubiquitin modifier ligase. This work sheds light on the overall organization of the full-length protein combining solution scattering data, integrative modeling, and single-molecule experiments. We show that KAP1 is an elongated antiparallel dimer with an asymmetry at the C-terminal domains. This conformation is consistent with the finding that the Really Interesting New Gene (RING) domain contributes to KAP1 auto-SUMOylation. Importantly, this intrinsic asymmetry has key functional implications for the KAP1 network of interactions, as the heterochromatin protein 1 (HP1) occupies only one of the two putative HP1 binding sites on the KAP1 dimer, resulting in an unexpected stoichiometry, even in the context of chromatin fibers. |
リンク | Life Sci Alliance / PubMed:31427381 / PubMed Central |
手法 | SAS (X-ray synchrotron) |
構造データ | SASDER7: KRAB-associated protein 1 (KAP1); TRIM28, amino acids 23-812 SASDEV6: SASDEW6: |
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