Abstract
SAMHD1 (sterile α motif and histidine (H) aspartate (D) domain-containing protein 1) is known for its antiviral activity of hydrolysing deoxynucleotides required for virus replication. Daddacha et al. identify a hydrolase-independent, moonlighting function of SAMHD1 that facilitates homologous recombination of DNA double-strand breaks (DSBs) by promoting recruitment of C-terminal binding protein interacting protein (CTIP), a DNA-end resection factor, to damaged DNA. These findings could benefit anticancer treatment.
Highlights
SAMHD1 (sterile a motif and histidine (H) aspartate (D) domain-containing protein 1) is known for its antiviral activity of hydrolysing deoxynucleotides required for virus replication
double-strand breaks (DSBs) are highly cytotoxic lesions mostly repaired through two major pathways: one, termed nonhomologous end-joining (NHEJ), can be error prone, acts throughout the cell cycle and involves direct religation of broken DNA ends
The resulting 30 single-stranded DNA overhangs are coated by the ssDNA-binding protein RPA, which is replaced by the RAD51 recombinase to form nucleoprotein filaments that mediate strand invasion, followed by final homologous recombination (HR) steps (Figure 1A) [1,2,3]
Summary
SAMHD1 (sterile a motif and histidine (H) aspartate (D) domain-containing protein 1) is known for its antiviral activity of hydrolysing deoxynucleotides required for virus replication. Repaired damage can lead to cell death, genome instability, and cancer. DSBs are highly cytotoxic lesions mostly repaired through two major pathways: one, termed nonhomologous end-joining (NHEJ), can be error prone, acts throughout the cell cycle and involves direct religation of broken DNA ends. Resection relies on recruitment of CTIP ( known as RBBP8) to DSBs to activate the MRE11– RAD50–NBS1 (MRN) DNA nuclease complex.
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