KAP1 is an antiparallel dimer with a functional asymmetry.
Life Sci Alliance
; 2(4)2019 08.
Article
in En
| MEDLINE
| ID: mdl-31427381
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.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Tripartite Motif-Containing Protein 28
Type of study:
Prognostic_studies
Limits:
Humans
Language:
En
Journal:
Life Sci Alliance
Year:
2019
Document type:
Article
Affiliation country: