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Published 15 August 2005. doi:10.1083/jcb.200502154
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 170, Number 4, 537-549
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Article

 A glue for heterochromatin maintenance : stable SUV39H1 binding to heterochromatin is reinforced by the SET domain



Ilke M. Krouwels, Karien Wiesmeijer, Tsion E. Abraham, Chris Molenaar, Nico P. Verwoerd, Hans J. Tanke, and Roeland W. Dirks

Department of Molecular Cell Biology, Leiden University Medical Center, 2333 AL Leiden, Netherlands

Correspondence to Roeland W. Dirks: r.w.dirks{at}lumc.nl

Trimethylation of histone H3 lysine 9 and the subsequent binding of heterochromatin protein 1 (HP1) mediate the formation and maintenance of pericentromeric heterochromatin. Trimethylation of H3K9 is governed by the histone methyltransferase SUV39H1. Recent studies of HP1 dynamics revealed that HP1 is not a stable component of heterochromatin but is highly mobile (Cheutin, T., A.J. McNairn, T. Jenuwein, D.M. Gilbert, P.B. Singh, and T. Misteli. 2003. Science. 299:721–725; Festenstein, R., S.N. Pagakis, K. Hiragami, D. Lyon, A. Verreault, B. Sekkali, and D. Kioussis. 2003. Science. 299:719–721). Because the mechanism by which SUV39H1 is recruited to and interacts with heterochromatin is unknown, we studied the dynamic properties of SUV39H1 in living cells by using fluorescence recovery after photobleaching and fluorescence resonance energy transfer. Our results show that a substantial population of SUV39H1 is immobile at pericentromeric heterochromatin, suggesting that, in addition to its catalytic activity, SUV39H1 may also play a structural role at pericentromeric regions. Analysis of SUV39H1 deletion mutants indicated that the SET domain mediates this stable binding. Furthermore, our data suggest that the recruitment of SUV39H1 to heterochromatin is at least partly independent from that of HP1 and that HP1 transiently interacts with SUV39H1 at heterochromatin.

C. Molenaar's present address is Developmental Genetics Laboratory, Cancer Research UK, London WC2A 3PX, England, UK.

Abbreviations used in this paper: 5-aza-C, 5-aza-2'deoxycytidine; BP, bandpass; dn, double null; FLIM, fluorescence lifetime imaging microscopy; FRET, fluorescence resonance energy transfer; HP1, heterochromatin protein 1; PMEF, primary mouse embryonic fibroblast; TSA, trichostatin A.


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