Abstract
The Chromatin Assembly Factor 1 is a heterotrimeric complex responsible for the nucleosome assembly during DNA replication and DNA repair. In humans, the largest subunit P150 is the major actor of this process. It has been recently considered as a tumor-associated protein due to its overexpression in many malignancies. Structural and functional studies targeting P150 are still limited and only scarce information about this subunit is currently available. Literature data and bioinformatics analysis assisted the identification of a stable DNA binding domain, encompassing residues from 721 to 860 of P150 within the full-length protein. This domain was recombinantly produced and in vitro investigated. An acidic region modulating its DNA binding ability was also identified and characterized. Results showed similarities and differences between the P150 and its yeast homologue, namely Cac-1, suggesting that, although sharing a common biological function, the two proteins may also possess different features.
Highlights
IntroductionPublisher’s Note: MDPI stays neutral with regard to jurisdictional claims in published maps and institutional affiliations
Zhang and coworkers identified the region 727–854 of human P150 as the one corresponding to Cac-1 winged helix domain (WHD) [42]
P150721–860 gene was cloned into pETM13 vector, allowing the expression of the protein with a His tag at its C-terminal part
Summary
Publisher’s Note: MDPI stays neutral with regard to jurisdictional claims in published maps and institutional affiliations. Genomic DNA is well packaged into a compact and ordered entity named nucleosome, the single unit of chromatin [1,2]. This repeating entity is formed by double-stranded DNA (145–147 bp) wrapped around an octamer of histones (a duplicate of H2A, H2B, H3, and H4) [3]. Nucleosomes undertake additional condensation stages to form the final level of compactness, leading to the chromatid of chromosome [4,5]
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