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)
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: |
https://repository.cshl.edu/id/eprint/27910 |
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