KAP1 is an antiparallel dimer with a natively functional asymmetry
Citations Over Time
Abstract
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.
Related Papers
- → The role of SUMOylation during development(2020)45 cited
- → Transcription of Giant DNA Complexed with Cationic Nanoparticles as a Simple Model of Chromatin(2006)32 cited
- → Effect of DNA Groove Binder Distamycin A upon Chromatin Structure(2011)20 cited
- Dynamic inorganic ion-protein interactions in structural organization of DNA of living cell nuclei.(1979)
- → PROTON NMR STUDY ON A TYPE II DNA BINDING PROTEIN HUα FROM <i>Escherichia coli</i> AND ITS COMPLEX WITH OLIGO DNA(1991)