AI Article Synopsis
- Oligomeric state determination of enzymes like RecQ helicases is crucial for understanding their catalytic functions, but there's still uncertainty about how these states relate to their biochemical activities.
- Researchers used single-molecule multi-color fluorescence imaging to study the Werner syndrome protein (WRN) and found it binds as a dimer to forked DNA and remains a dimer while unwinding it, but forms a tetramer at a replication fork and then dimerizes to activate fork regression.
- By selectively inhibiting WRN's helicase function on certain strands, they demonstrated how active dimers of WRN utilize ATP hydrolysis energy for both unwinding and regression tasks.
Article Abstract
The determination of the oligomeric state of functional enzymes is essential for the mechanistic understanding of their catalytic activities. RecQ helicases have diverse biochemical activities, but it is still unclear how their activities are related to their oligomeric states. We use single-molecule multi-color fluorescence imaging to determine the oligomeric states of Werner syndrome protein (WRN) during its unwinding and replication fork regression activities. We reveal that WRN binds to a forked DNA as a dimer, and unwinds it without any change of its oligomeric state. In contrast, WRN binds to a replication fork as a tetramer, and is dimerized during activation of replication fork regression. By selectively inhibiting the helicase activity of WRN on specific strands, we reveal how the active dimers of WRN distinctly use the energy of ATP hydrolysis for repetitive unwinding and replication fork regression.
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Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC9841404 | PMC |
| http://dx.doi.org/10.1093/nar/gkac1200 | DOI Listing |
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