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An RNA matchmaker protein regulates the activity of the long noncoding RNA HOTAIR
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Using quantitative mass spectrometry, we profiled the proteins that associate with We validated the interactions with HOTAIR via Western analysis after RNA.
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In breast cancers, overexpression of HOTAIR increases metastatic potential via the repression of many additional genes. The regulated expression of the genome requires the formation of facultative heterochromatin fHC Trojer and Reinberg , which stably represses transcription. Although heterochromatin is essential for normal human development, dysregulation can promote cancer by altered expression of oncogenic and tumor suppressor genes.
The recruitment of PRC2 to target genes results in the methylation of lysine 27 on histone 3 H3K27me , a histone mark that triggers formation of repressed chromatin Simon and Kingston PRC2 components are frequently up-regulated in multiple cancer types and can promote neoplastic transformation Varambally et al. However, PRC2 also readily binds to the nascent transcripts of actively transcribed genes Davidovich et al.
More recently, this lncRNA has been shown to associate with hundreds of additional sites in the genome and to initiate broad changes in gene expression when overexpressed Gupta et al. HOTAIR has been suggested to recruit both complexes to target sites to generate a repressed chromatin state Gupta et al. Although the two isoforms differ only by a amino acid amino-terminal sequence Burd et al.
These results are consistent with recent studies that revealed the promiscuous binding of PRC2 to numerous long RNA molecules Davidovich et al. Ratios of all identified proteins were plotted. D Schematic of the A2 and B1 proteins, which differ only by the unique B1 N-terminal domain encoded by exon 2. To identify new interaction partners of HOTAIR that may govern its activity, we performed an unbiased comparative mass spectrometry analysis of all stably associated proteins in the RNA pulldown experiment Fig.
B1 differs from its A2 isoform solely by the inclusion of an exon encoding twelve amino acids at the N-terminus Fig.