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TitleKAP1 is an antiparallel dimer with a functional asymmetry.
Journal, issue, pagesLife Sci Alliance, Vol. 2, Issue 4, Year 2019
Publish dateAug 19, 2019
AuthorsGiulia 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 AbstractKAP1 (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.
External linksLife Sci Alliance / PubMed:31427381 / PubMed Central
MethodsSAS (X-ray synchrotron)
Structure data

SASDER7: KRAB-associated protein 1 (KAP1); TRIM28, amino acids 23-812
Method: SAXS/SANS

SASDEV6:
KRAB-associated protein 1 (KAP1); TRIM28; full length protein
Method: SAXS/SANS

SASDEW6:
KRAB-associated protein 1, (KAP1); TRIM28; 23-418 RBCC domain
Method: SAXS/SANS

Source
  • Homo sapiens (human)

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