Major satellite repeat RNA stabilize heterochromatin retention of Suv39h enzymes by RNA-nucleosome association and RNA: DNA hybrid formation

Oscar Velazquez Camacho, Carmen Galan, Kalina Swist-Rosowska, Reagan Ching, Michael Gamalinda, Fethullah Karabiber, Inti De La Rosa-Velazquez, Bettina Engist, Birgit Koschorz, Nicholas Shukeir, Megumi Onishi-Seebacher, Suzanne Van De Nobelen, Thomas Jenuwein*

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

38 Citations (Scopus)

Abstract

The Suv39h1 and Suv39h2 histone lysine methyltransferases are hallmark enzymes at mammalian heterochromatin. We show here that the mouse Suv39h2 enzyme differs from Suv39h1 by containing an N-terminal basic domain that facilitates retention at mitotic chromatin and provides an additional affinity for major satellite repeat RNA. To analyze an RNA-dependent interaction with chromatin, we purified native nucleosomes from mouse ES cells and detect that Suv39h1 and Suv39h2 exclusively associate with poly-nucleosomes. This association was attenuated upon RNaseH incubation and entirely lost upon RNaseA digestion of native chromatin. Major satellite repeat transcripts remain chromatin-associated and have a secondary structure that favors RNA:DNA hybrid formation. Together, these data reveal an RNA-mediated mechanism for the stable chromatin interaction of the Suv39h KMT and suggest a function for major satellite noncoding RNA in the organization of an RNA-nucleosome scaffold as the underlying structure of mouse heterochromatin.
Original languageEnglish
Article numbere25293
JournaleLife
Volume6
DOIs
Publication statusPublished - 1 Aug 2017

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    Camacho, O. V., Galan, C., Swist-Rosowska, K., Ching, R., Gamalinda, M., Karabiber, F., ... Jenuwein, T. (2017). Major satellite repeat RNA stabilize heterochromatin retention of Suv39h enzymes by RNA-nucleosome association and RNA: DNA hybrid formation. eLife, 6, [e25293]. https://doi.org/10.7554/eLife.25293