SAF-A Regulates Interphase Chromosome Structure through Oligomerization with Chromatin-Associated RNAs.

ABSTRACT: Higher eukaryotic chromosomes are organized into topologically constrained functional domains; however, the molecular mechanisms required to sustain these complex interphase chromatin structures are unknown. A stable matrix underpinning nuclear organization was hypothesized, but the idea was abandoned as more dynamic models of chromatin behavior became prevalent. Here, we report that scaffold attachment factor A (SAF-A), originally identified as a structural nuclear protein, interacts with chromatin-associated RNAs (caRNAs) via its RGG domain to regulate human interphase chromatin structures in a transcription-dependent manner. Mechanistically, this is dependent on SAF-A's AAA⁺ ATPase domain, which mediates cycles of protein oligomerization with caRNAs, in response to ATP bindin

SUBMITTER: Nozawa RS 

PROVIDER: S-EPMC5473940 | biostudies-literature | 2017 Jun

REPOSITORIES: biostudies-literature