Chromatin remodeling enzymes act to dynamically regulate gene accessibility. In many cases, these enzymes function as large multi-component complexes that, in general, comprise a central ATP-dependent Snf2-family helicase that is decorated with a variable number of regulatory subunits. The Nucleosome Remodeling and Deacetylase complex (NuRD), which is essential for normal development in higher organisms, is one such macromolecular machine. The NuRD complex comprises approximately 10 subunits, including the histone deacetylases 1 and 2 (HDAC1 and HDAC2), and is defined by the presence of a CHD-family remodeling enzyme - most commonly Chromodomain Helicase DNA-binding protein 4 (CHD4). The existing paradigm holds that CHD4 acts as the central hub upon which the complex is built. We show here that this paradigm does not, in fact, hold and that CHD4 is only a peripheral and dynamic component of the NuRD complex. A complex lacking CHD4 that has HDAC activity can exist as a stable species in cells. The addition of recombinant CHD4 to this Nucleosome Deacetylase (NuDe) complex reconstitutes a NuRD complex with nucleosome remodeling activity. These data are an important step towards understanding the architecture of the NuRD complex.