FOG-1 recruits the NuRD repressor complex to mediate transcriptional repression by GATA-1

Hong, W., Nakazawa, M., Chen, Y. Y., Kori, R., Vakoc, C. R., Rakowski, C., Blobel, G. A. (2005) FOG-1 recruits the NuRD repressor complex to mediate transcriptional repression by GATA-1. Embo Journal, 24 (13). pp. 2367-2378. ISSN 0261-4189

URL: http://www.ncbi.nlm.nih.gov/pubmed/15920470
DOI: 10.1038/sj.emboj.7600703

Abstract

Transcription factor GATA-1 and its cofactor FOG-1 coordinate erythroid cell maturation by activating erythroid-specific genes and repressing genes associated with the undifferentiated state. Here we show that FOG-1 binds to the NuRD corepressor complex in vitro and in vivo. The interaction is mediated by a small conserved domain at the extreme N-terminus of FOG-1 that is necessary and sufficient for NuRD binding. This domain defines a novel repression module found in diverse transcriptional repressors. NuRD is present at GATA-1/FOG-1-repressed genes in erythroid cells in vivo. Point mutations near the N-terminus of FOG-1 that abrogate NuRD binding block gene repression by FOG-1. Finally, the ability of GATA-1 to repress transcription was impaired in erythroid cells expressing mutant forms of FOG-1 that are defective for NuRD binding. Together, these studies show that FOG-1 and likely other FOG-like proteins are corepressors that link GATA factors to histone deacetylation and nucleosome remodeling. © 2005 European Molecular Biology Organization | All Rights Reserved.

Item Type: Paper
Uncontrolled Keywords: Chromatin FOG-1 GATA-1 Gene repression NuRD histone deacetylase protein fog 1 transcription factor GATA 1 unclassified drug zinc finger protein amino terminal sequence animal cell article cell maturation controlled study deacetylation erythroid cell human human cell nonhuman nucleosome NuRD repressor complex point mutation priority journal protein binding protein domain protein expression protein protein interaction repressor gene transcription regulation transcription repression Amino Acid Motifs Amino Acid Sequence Animals Carrier Proteins Cells, Cultured Cercopithecus aethiops DNA-Binding Proteins Erythroid Specific DNA Binding Factors GATA1 Transcription Factor Gene Silencing Histone Deacetylases Mice Molecular Sequence Data N-Glycosyl Hydrolases Nuclear Proteins Protein Structure, Tertiary Proto-Oncogene Proteins c-kit Repressor Proteins Sequence Homology, Amino Acid Transcription Factors Transcription, Genetic
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification > transcription
bioinformatics > genomics and proteomics > genetics & nucleic acid processing
bioinformatics > genomics and proteomics
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 > DNA binding protein
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification > genes, structure and function > gene regulation
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification > genes, structure and function > gene regulation

bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification > genes, structure and function
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein receptor
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types
CSHL Authors:
Communities: CSHL labs > Vakoc lab
Depositing User: CSHL Librarian
Date Deposited: 19 Mar 2012 18:28
Last Modified: 13 Mar 2013 20:32
Related URLs:
URI: http://repository.cshl.edu/id/eprint/25395

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