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A more recent version of this article appeared on June 1, 2004
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Submitted on November 19, 2003
Revised on March 19, 2004
Accepted on March 19, 2004
1 Department for Molecular Biology, Institute of Molecular Biotechnology, Jena, Germany
2 Carl-Zeiss Jena GmbH, Advanced Imaging Microscopy, Jena, Germany
3 Department for Single-Cell and Single-Molecule Techniques, Institute of Molecular Biotechnology, Jena, Germany
* Corresponding author. E-mail address: phemmer{at}imb-jena.de.
Heterochromatin protein 1 (HP1) is a conserved nonhistone chromosomal protein with functions in euchromatin and heterochromatin. Here we investigated the diffusional behaviors of HP1 isoforms in mammalian cells. Using fluorescence correlation spectroscopy (FCS) and fluorescence recovery after photobleaching (FRAP) we found that in interphase cells most HP1 molecules (50-80%) are highly mobile (recovery halftime: t1/2 
0.9 s; diffusion coefficient: D 0.6 - 0.7 µm2s-1). Twenty to forty percent of HP1 molecules appear to be incorporated into stable, slow moving oligomeric complexes (t1/2 10 s), and constitutive heterochromatin of all mammalian cell types analyzed contain 5-7% of very slow HP1 molecules. The amount of very slow HP1 molecules correlated with the chromatin condensation state, mounting to more than 44% in condensed chromatin of transcriptionally silent cells. During mitosis 8-14% of GFP-HP1
, but not the other isoforms, are very slow within pericentromeric heterochromatin, indicating an isoform-specific function of HP1 in heterochromatin of mitotic chromosomes. These data suggest that mobile as well as very slow populations of HP1 may function in concert to maintain a stable conformation of constitutive heterochromatin throughout the cell cycle.
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