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KAP1 is an antiparallel dimer with a functional asymmetry

Abstract : 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 SUMO ligase. This work sheds light on the overall organization of the full-length protein combining solution scattering diffraction data, integrative modeling and single-molecule experiments. We show that KAP1 is an elongated antiparallel dimer with a native asymmetry at the C-terminal domain. This conformation supports our finding that the 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.
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Contributor : Sergei Grudinin <>
Submitted on : Thursday, September 19, 2019 - 4:54:27 AM
Last modification on : Tuesday, November 24, 2020 - 5:04:04 PM

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Giulia Fonti, Maria Marcaida, Louise Bryan, Sylvain Träger, Alexandra Kalantzi, et al.. KAP1 is an antiparallel dimer with a functional asymmetry. Life Science Alliance, Life Science Alliance LLC, 2019, 2 (4), pp.e201900349. ⟨10.26508/lsa.201900349⟩. ⟨hal-02291553⟩



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