A Human Tumor Virus Recruits HSP70 Chaperone to Remodel Its Replisome on DNA

sT recruits dimeric HSP70 to bridge sT and MCV large T on DNA, enabling LT remodeling into a functional double-hexameric helicase.

• Why it matters: Efficient LT-initiated replication depends on sT, but how sT engages host chaperones to remodel the viral replisome was unclear.
• What they did: Using single-molecule imaging and FRET, the study tested sT–HSP70 recruitment and LT remodeling, then disrupted the LT–HSP70–HSP70–sT interaction with HSP70 inhibitors or DnaJ-domain mutations.
• The result: Disruption collapsed the LT–HSP70–HSP70–sT complex, abolishing sT-enhanced LT dodecamerization and ATP-dependent DNA unwinding; virus-free MCM3/4/6 assembly in nuclear extracts also recruited HSP70 to DNA.

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