Chromodomain-helicase-DNA-binding domain proteins have been identified in a variety of organisms. This family of nine proteins is divided into three separate subfamilies: subfamily I, subfamily II, and subfamily III. All CHD proteins contain two tandem amino-terminal chromodomains, a SWI/SNF-related ATPase domain, and a carboxy-terminal DNA-binding domain. The chromodomains facilitate binding to methylated lysine residues of histone proteins and confer interactions with specific regions of chromatin. The SWI/SNF-related ATPase domain utilizes energy from ATP hydrolysis to modify chromatin structure. CHD proteins are often found in large, multiprotein complexes with their transcriptional activation or repression activity governed by other proteins within the complex. CHD3 and CHD4 are central components of the nucleosome remodeling and histone deacetylase transcriptional repressor complex, which also contains HDAC1, HDAC2, RBAP48, RBAP46, MTA1, MTA2, MTA3, and MBD3. Both CHD3 and CHD4 contain two plant homeodomain zinc finger domains that bind directly to HDAC1 and HDAC2.
[1] Hall, J.A. and Georgel, P.T. (2007) Biochem Cell Biol 85, 463-76.
[2] Marfella, C.G. and Imbalzano, A.N. (2007) Mutat Res 618, 30-40.
[3] Tong, J.K. et al. (1998) Nature 395, 917-21.
[4] Xue, Y. et al. (1998) Mol Cell 2, 851-61.
[5] Zhang, Y. et al. (1998) Cell 95, 279-89.
[6] Bowen, N.J. et al. (2004) Biochim Biophys Acta 1677, 52-7.
[7] Jones, P.L. et al. (1998) Nat Genet 19, 187-91.
[8] Fujita, N. et al. (2003) Cell 113, 207-19.
