In:
Life Science Alliance, Life Science Alliance, LLC, Vol. 2, No. 4 ( 2019-08), p. e201900349-
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 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.
Type of Medium:
Online Resource
ISSN:
2575-1077
DOI:
10.26508/lsa.201900349
Language:
English
Publisher:
Life Science Alliance, LLC
Publication Date:
2019
detail.hit.zdb_id:
2948687-7
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