A switch in mitotic histone H4 lysine 20 methylation status is linked to M phase defects upon loss of HCF-1

Julien, E., Herr, W. (2004) A switch in mitotic histone H4 lysine 20 methylation status is linked to M phase defects upon loss of HCF-1. Mol Cell, 14 (6). pp. 713-25. ISSN 1097-2765 (Print)

URL: http://www.sciencedirect.com/science/article/pii/S...
DOI: 10.1016/j.molcel.2004.06.008

Abstract

The abundant chromatin-associated human factor HCF-1 is a heterodimeric complex of HCF-1N and HCF-1C subunits that are essential for two stages of the cell cycle. The HCF-1N subunit promotes G1 phase progression, whereas the HCF-1C subunit ensures proper cytokinesis at completion of M phase. How the HCF-1C subunit functions is unknown. Here, we show that HCF-1C subunit depletion causes extensive mitotic defects, including a switch from monomethyl to dimethyl lysine 20 of histone H4 (H4-K20) and defective chromosome alignment and segregation. Consistent with these activities, the HCF-1C subunit can associate with chromatin independently of the HCF-1N subunit and regulates the expression of the H4-K20 methyltransferase PR-Set7. Indeed, upregulation of PR-Set7 expression upon loss of HCF-1 leads to improper mitotic H4-K20 methylation and cytokinesis defects. These results establish the HCF-1C subunit as an important M phase regulator and suggest that H4-K20 methylation status contributes to chromosome behavior during mitosis and proper cytokinesis.

Item Type: Paper
Uncontrolled Keywords: Cell Division physiology Cell Line Tumor Chromatin metabolism Cytokinesis Hela Cells Histone-Lysine N-Methyltransferase metabolism Histones chemistry metabolism Host Cell Factor C1 Humans Lysine metabolism Methylation Mitosis physiology RNA Messenger metabolism RNA Small Interfering metabolism Transcription Factors genetics/metabolism physiology Up-Regulation
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification > Chromatin dynamics
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > methyltransferase
CSHL Authors:
Depositing User: CSHL Librarian
Date Deposited: 01 Feb 2012 16:03
Last Modified: 01 Feb 2012 16:03
URI: http://repository.cshl.edu/id/eprint/22405

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