Real-time compaction of nanoconfined DNA by an intrinsically disordered macromolecular counterion.
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ABSTRACT: We demonstrate how a recently developed nanofluidic device can be used to study protein-induced compaction of genome-length DNA freely suspended in solution. The protein we use in this study is the hepatitis C virus core protein (HCVcp), which is a positively charged, intrinsically disordered protein. Using nanofluidic devices in combination with fluorescence microscopy, we observe that protein-induced compaction preferentially begins at the ends of linear DNA. This observation would be difficult to make with many other single-molecule techniques, which generally require the DNA ends to be anchored to a substrate. We also demonstrate that this protein-induced compaction is reversible and can be dynamically modulated by exposing the confined DNA molecules to solutions containing either HCVc
SUBMITTER: Sharma R
PROVIDER: S-EPMC7577930 | biostudies-literature | 2020 Nov
REPOSITORIES: biostudies-literature
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