ChromodomainhelicaseDNAbinding

Chromodomain-helicase DNA-binding proteins, often abbreviated as CHD proteins, are a family of ATP-dependent molecular motors that play crucial roles in the regulation of gene expression and genome stability. These proteins are characterized by the presence of a chromodomain at their N-terminus, which is known to bind to methylated lysine residues on histone tails, and a helicase-SANT-associated (HSA) domain. The core enzymatic activity of CHD proteins lies in their ATPase and DNA-helicase domains, which enable them to remodel chromatin.

CHD proteins function as ATP-dependent chromatin remodelers. By utilizing the energy from ATP hydrolysis, they can alter the structure of nucleosomes, the basic units of chromatin. This remodeling can involve sliding nucleosomes along DNA, ejecting them entirely, or restructuring them, thereby influencing the accessibility of DNA to transcription factors and other regulatory proteins. This mechanism is central to their role in gene activation and repression. Furthermore, some CHD proteins have been implicated in DNA repair pathways, highlighting their involvement in maintaining genomic integrity.

Dysregulation of CHD protein function has been linked to various human diseases, including cancer and developmental disorders. Mutations or aberrant expression of certain CHD proteins can lead to inappropriate gene silencing or activation, contributing to uncontrolled cell proliferation and other pathological conditions. Research into the precise mechanisms of CHD protein action and their involvement in disease is ongoing, with the aim of developing targeted therapeutic strategies.