JCB logo
Keystone Symposia 2009 Meetings
  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents
Published 15 August 2005. doi:10.1083/jcb.200502154
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 170, Number 4, 537-549
This Article
Right arrow Full Text
Right arrow Full Text (PDF, 5093K)
Right arrow PPT slides of all figures
Right arrow Alert me when this article is cited
Right arrow Citation Map
Services
Right arrow Email this article
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new content in the JCB
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Krouwels, I. M.
Right arrow Articles by Dirks, R. W.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Krouwels, I. M.
Right arrow Articles by Dirks, R. W.
Right arrowPubmed/NCBI databases
*Gene*GEO Profiles
*HomoloGene*Protein
*UniGene
*Compound via MeSH
*Substance via MeSH
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

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.


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:



  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents