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

Autor: Rajashree Kori, Gerd A. Blobel, Carrie Rakowski, Christopher R. Vakoc, Minako Nakazawa, Wei Hong, Ying-Yu Chen
Rok vydání: 2004
Předmět:
genetic structures
Transcription
Genetic
Amino Acid Motifs
Molecular Sequence Data
Repressor
General Biochemistry
Genetics and Molecular Biology
Histone Deacetylases
Article
Mice
Chlorocebus aethiops
Animals
Point Mutation
RBBP4
GATA1 Transcription Factor
Amino Acid Sequence
Gene Silencing
Molecular Biology
Psychological repression
Transcription factor
N-Glycosyl Hydrolases
Cells
Cultured
Genetics
General Immunology and Microbiology
Erythroid-Specific DNA-Binding Factors
biology
Sequence Homology
Amino Acid
General Neuroscience
Nuclear Proteins
Mi-2/NuRD complex
Protein Structure
Tertiary
DNA-Binding Proteins
Repressor Proteins
Proto-Oncogene Proteins c-kit
Histone
biology.protein
Carrier Proteins
Corepressor
Mi-2 Nucleosome Remodeling and Deacetylase Complex
Protein Binding
Transcription Factors
Zdroj: The EMBO journal. 24(13)
ISSN: 0261-4189
Popis: 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.
Databáze: OpenAIRE
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