ASF1A Human

ASF1A is a key component of the histone donor complex, which interacts with histones H3 and H4 . It works in conjunction with chromatin assembly factors to facilitate the deposition, exchange, and removal of histones during nucleosome assembly and disassembly . This process is vital for maintaining chromatin structure and function during DNA replication and repair .

ASF1A also promotes homologous recombination-mediated repair of double-strand breaks (DSBs) at stalled or collapsed replication forks . It achieves this by mediating histone replacement at DSBs, leading to the recruitment of the MMS22L-TONSL complex and subsequent loading of RAD51 .

The protein is involved in both replication-dependent and replication-independent chromatin assembly . It cooperates with chromatin assembly factor 1 (CAF-1) to promote replication-dependent chromatin assembly and with HIRA to promote replication-independent chromatin assembly . Additionally, ASF1A is involved in the nuclear import of the histone H3-H4 dimer together with importin-4 (IPO4) .

Mutations or dysregulation of ASF1A have been associated with various diseases, including Spastic Paraplegia 7, Autosomal Recessive, and Fanconi Anemia, Complementation Group I . Understanding the function and regulation of ASF1A can provide insights into the mechanisms underlying these diseases and potentially lead to the development of targeted therapies.

ASF1A is widely studied in the context of chromatin biology and epigenetics. Its role in histone chaperoning makes it a critical factor in understanding chromatin dynamics and gene regulation. Recombinant ASF1A proteins are used in various research applications to study these processes in detail .