Human Sin3 deacetylase and trithorax-related Set1/Ash2 histone H3-K4 methyltransferase are tethered together selectively by the cell-proliferation factor HCF-1

Wysocka, J., Myers, M. P., Laherty, C. D., Eisenman, R. N., Herr, W. (April 2003) Human Sin3 deacetylase and trithorax-related Set1/Ash2 histone H3-K4 methyltransferase are tethered together selectively by the cell-proliferation factor HCF-1. Genes and Development, 17 (7). pp. 896-911. ISSN 08909369 (ISSN)

URL: http://www.ncbi.nlm.nih.gov/pubmed/12670868
DOI: 10.1101/gad.252103

Abstract

The abundant and chromatin-associated protein HCF-1 is a critical player in mammalian cell proliferation as well as herpes simplex virus (HSV) transcription. We show here that separate regions of HCF-1 critical for its role in cell proliferation associate with the Sin3 histone deacetylase (HDAC) and a previously uncharacterized human trithorax-related Set1/Ash2 histone methyltransferase (HMT). The Set1/Ash2 HMT methylates histone H3 at Lys 4 (K4), but not if the neighboring K9 residue is already methylated. HCF-1 tethers the Sin3 and Set1/Ash2 transcriptional regulatory complexes together even though they are generally associated with opposite transcriptional outcomes: repression and activation of transcription, respectively. Nevertheless, this tethering is context-dependent because the transcriptional activator VP16 selectively binds HCF-1 associated with the Set1/Ash2 HMT complex in the absence of the Sin3 HDAC complex. These results suggest that HCF-1 can broadly regulate transcription, both positively and negatively, through selective modulation of chromatin structure.

Item Type: Paper
Uncontrolled Keywords: Binding Sites Cell Division/physiology DNA-Binding Proteins/genetics Hela Cells Herpes Simplex Virus Protein Vmw65/metabolism Histone Deacetylases/ genetics/isolation & purification/metabolism Histone-Lysine N-Methyltransferase Host Cell Factor C1 Humans Kinetics Methyltransferases/ genetics Proteins/ metabolism Saccharomyces cerevisiae Proteins/genetics Transcription Factors/genetics Transfection
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes
organism description > virus > herpes simplex virus
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > histone
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes > histone deacetylase
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > methyltransferase
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types
organism description > virus
CSHL Authors:
Communities: CSHL labs > Herr lab
Depositing User: Matt Covey
Date: 1 April 2003
Date Deposited: 28 Jun 2013 18:50
Last Modified: 28 Jun 2013 18:50
PMCID: PMC196026
Related URLs:
URI: http://repository.cshl.edu/id/eprint/27910

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