Serine protease FAM111A

Definition

Single-stranded DNA-binding serine protease that mediates the proteolytic cleavage of covalent DNA-protein cross-links (DPCs) during DNA synthesis, thereby playing a key role in maintaining genomic integrity. DPCs are highly toxic DNA lesions that interfere with essential chromatin transactions, such as replication and transcription, and which are induced by reactive agents, such as UV light or formaldehyde. Protects replication fork from stalling by removing DPCs, such as covalently trapped topoisomerase 1 (TOP1) adducts on DNA lesion, or poly(ADP-ribose) polymerase 1 (PARP1)-DNA complexes trapped by PARP inhibitors. Required for PCNA loading on replication sites. Promotes S-phase entry and DNA synthesis.; (Microbial infection) May directly function at replication forks, explaining why Simian virus 40 (SV40) interacts with FAM111A to overcome host range restriction.

References:

[1]. Yusuke Kojima, et al. FAM111A protects replication forks from protein obstacles via its trypsin-like domain. Nat Commun. 2020 Mar 12;11(1):1318. [Content Brief]

[2]. Debrah A Fine, et al. Identification of FAM111A as an SV40 host range restriction and adenovirus helper factor. PLoS Pathog. 2012;8(10):e1002949. [Content Brief]

[3]. Constance Alabert, et al. Nascent chromatin capture proteomics determines chromatin dynamics during DNA replication and identifies unknown fork components. Nat Cell Biol. 2014 Mar;16(3):281-93. [Content Brief]

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