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Plant Cell Advance Online Publication
Published on December 16, 2005; 10.1105/tpc.105.036855

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Received August 29, 2005
Returned for revision November 1, 2005
Accepted November 16, 2005

Different Domains Control the Localization and Mobility of LIKE HETEROCHROMATIN PROTEIN1 in Arabidopsis Nuclei

Assaf Zemach 1, Yan Li 1, Hagit Ben-Meir 1, Moran Oliva 2, Assaf Mosquna 2, Vladimir Kiss 1, Yigal Avivi 1, Nir Ohad 2, and Gideon Grafi 1*

1 Department of Plant Sciences, Weizmann Institute of Science, Rehovot, 76100 Israel
2 Department of Plant Sciences, Tel Aviv University, Tel Aviv, IL-69978 Israel

* To whom correspondence should be addressed. E-mail: ggrafi{at}agri.gov.il.

Plants possess a single gene for the structurally related HETEROCHROMATIN PROTEIN1 (HP1), termed LIKE-HP1 (LHP1). We investigated the subnuclear localization, binding properties, and dynamics of LHP1 proteins in Arabidopsis thaliana cells. Transient expression assays showed that tomato (Solanum lycopersicum) LHP1 fused to green fluorescent protein (GFP; Sl LHP1-GFP) and Arabidopsis LHP1 (At LHP1-GFP) localized to heterochromatic chromocenters and showed punctuated distribution within the nucleus; tomato but not Arabidopsis LHP1 was also localized within the nucleolus. Mutations of aromatic cage residues that recognize methyl K9 of histone H3 abolished their punctuated distribution and localization to chromocenters. Sl LHP1-GFP plants displayed cell type-dependent subnuclear localization. The diverse localization pattern of tomato LHP1 did not require the chromo shadow domain (CSD), whereas the chromodomain alone was insufficient for localization to chromocenters; a nucleolar localization signal was identified within the hinge region. Fluorescence recovery after photobleaching showed that Sl LHP1 is a highly mobile protein whose localization and retention are controlled by distinct domains; retention at the nucleolus and chromocenters is conferred by the CSD. Our results imply that LHP1 recruitment to chromatin is mediated, at least in part, through interaction with methyl K9 and that LHP1 controls different nuclear processes via transient binding to its nuclear sites.






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