Directed targeting of chromatin to the nuclear lamina is mediated by chromatin state and A-type lamins

Jennifer C. Harr, Teresa Romeo Luperchio, Xianrong Wong, Erez Cohen, Sarah J. Wheelan, Karen L. Reddy

Research output: Contribution to journalArticle

Abstract

Nuclear organization has been implicated in regulating gene activity. Recently, large developmentally regulated regions of the genome dynamically associated with the nuclear lamina have been identified. However, little is known about how these laminaassociated domains (LADs) are directed to the nuclear lamina. We use our tagged chromosomal insertion site system to identify small sequences from borders of fibroblastspecific variable LADs that are sufficient to target these ectopic sites to the nuclear periphery. We identify YY1 (Ying-Yang1) binding sites as enriched in relocating sequences. Knockdown of YY1 or lamin A/C, but not lamin A, led to a loss of lamina association. In addition, targeted recruitment of YY1 proteins facilitated ectopic LAD formation dependent on histone H3 lysine 27 trimethylation and histone H3 lysine di- and trimethylation. Our results also reveal that endogenous loci appear to be dependent on lamin A/C, YY1, H3K27me3, and H3K9me2/3 for maintenance of lamina-proximal positioning.

Original languageEnglish (US)
Pages (from-to)33-52
Number of pages20
JournalJournal of Cell Biology
Volume208
Issue number1
DOIs
StatePublished - Jan 1 2015

ASJC Scopus subject areas

  • Cell Biology

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