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.