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

“A Human Tumor Virus Recruits HSP70 Chaperone to Remodel Its Replisome on DNA” (2026), by Li Wan et al. Genetics and Biochemistry research paper. Original abstract below, unchanged. A free PDF is available.

- Authors: Li Wan, Xiaochen Li, Paul Vittot, Jeffrey L. Brodsky, Peter Wipf, Patrick S. Moore, Yuan Chang
- Published: November 9, 2026
- Field: Genetics and Biochemistry
- DOI: https://doi.org/10.64898/2026.11.05.764654
- Free PDF: https://www.biorxiv.org/content/biorxiv/early/2026/11/09/2026.11.05.764654.full.pdf

## Abstract

Human Merkel cell polyomavirus (MCV) large T (LT) protein functions as a replication helicase analogous to the cellular MCM complex but requires a second MCV protein, small T (sT), for efficient LT-initiated replication. Both LT and sT encode highly-conserved DnaJ domains that bind to the cellular refolding molecule, heat shock protein 70 (HSP70). Using single-molecule imaging and FRET, we find that sT recruits dimeric HSP70 to serve as a molecular bridge between sT and LT on DNA and that this complex facilitates remodeling LT into a functional double-hexameric helicase. Disruption of LT-HSP70-HSP70-sT interaction with HSP70 inhibitors or by mutations to the LT-sT DnaJ domains collapse the LT-HSP70-HSP70-sT complex, abolishing sT-enhanced LT dodecamerization and ATP-dependent DNA unwinding. Assembly of virus-free mammalian MCM3, MCM4 and MCM6 in nuclear extracts similarly recruits HSP70 to DNA suggesting that Hsp70 remodeling is used for efficient eukaryotic assembly of the multi-protein replication machinery.

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