CHRAC1 Human

CHRAC1 is a histone-fold protein that interacts with other histone-fold proteins to bind DNA in a sequence-independent manner . These histone-fold protein dimers combine within larger enzymatic complexes for DNA transcription, replication, and packaging . The CHRAC1 protein forms a complex with DNA polymerase epsilon subunit POLE3 and binds naked DNA, which is then incorporated into chromatin . This process is aided by the nucleosome remodeling activity of ISWI/SNF2H and ACF1 .

The primary function of CHRAC1 is to facilitate chromatin remodeling, which is essential for various DNA-dependent processes such as transcription, replication, and repair . The chromatin remodeling complex, which includes CHRAC1, preferentially binds DNA through the CHRAC1-POLE3 heterodimer and possesses ATP-dependent nucleosome-remodeling activity . This activity is crucial for maintaining the dynamic nature of chromatin, allowing for the proper regulation of gene expression and other DNA-related processes.

The CHRAC1 gene is located on chromosome 8 in humans . It has several aliases, including CHRAC15, YCL1, and DNA Polymerase Epsilon Subunit P15 . The gene is highly conserved across different species, indicating its essential role in cellular processes.

Mutations or dysregulation of the CHRAC1 gene can potentially lead to various genetic disorders and diseases. Given its role in DNA transcription and replication, any abnormalities in CHRAC1 function can disrupt normal cellular processes and contribute to the development of diseases .

CHRAC1 is a subject of ongoing research, particularly in the fields of genetics and molecular biology. Understanding the mechanisms by which CHRAC1 and its associated complexes regulate chromatin accessibility can provide insights into the fundamental processes of gene expression and genome stability. Additionally, recombinant forms of CHRAC1 are used in research to study its function and interactions with other proteins and DNA.