The hinge domain of the epigenetic repressor, Smchd1, adopts an unconventional homodimeric configuration
- Author(s)
- Chen, K; Czabotar, PE; Blewitt, ME; Murphy, JM;
- Details
- Publication Year 2016-03-15,Volume 473,Issue #6,Page 733-42
- Journal Title
- Biochem J
- Publication Type
- Journal Article
- Abstract
- The structural maintenance of chromosome (SMC) proteins are fundamental to chromosome organization. They share a characteristic domain structure, featuring a central SMC hinge domain that is critical for forming SMC dimers and interacting with nucleic acids. The structural maintenance of chromosomes flexible hinge domain containing 1 (Smchd1) is a noncanonical member of the SMC family. While it has been well established that Smchd1 serves crucial roles in epigenetic silencing events implicated in development and disease, much less is known about the structure and function of Smchd1 protein. Recently, we demonstrated that the C-terminal hinge domain of Smchd1 forms a nucleic acid-binding homodimer, however, it is unclear how the protomers are assembled within the hinge homodimer and how the full-length Smchd1 protein is organised with respect to the hinge region. Here, by employing small-angle X-ray scattering (SAXS) we demonstrate that the hinge domain of Smchd1 likely adopts an unconventional homodimeric arrangement augmented by a coiled-coil formed between the two monomers. Such a dimeric structure differs markedly from that of archetypical SMC proteins, raising the possibility that Smchd1 binds chromatin in an unconventional manner.
- Publisher
- Portland Press
- Research Division(s)
- Molecular Medicine; Structural Biology; Cell Signalling And Cell Death
- PubMed ID
- 26733688
- Publisher's Version
- https://doi.org/10.1042/BJ20151049
- NHMRC Grants
- NHMRC/1045936, NHMRC/1079700,
- Terms of Use/Rights Notice
- Refer to copyright notice on published article.
Creation Date: 2016-01-29 11:46:00
Last Modified: 2016-05-09 12:46:57