Skip to main content

Research Repository

Advanced Search

All Outputs (3)

A Tryptophan ‘Gate’ in the CRISPR-Cas3 Nuclease Controls ssDNA Entry into the Nuclease Site, That When Removed Results in Nuclease Hyperactivity (2021)
Journal Article
He, L., Matošević, Z. J., Mitić, D., Markulin, D., Killelea, T., Matković, M., …Bolt, E. L. (2021). A Tryptophan ‘Gate’ in the CRISPR-Cas3 Nuclease Controls ssDNA Entry into the Nuclease Site, That When Removed Results in Nuclease Hyperactivity. International Journal of Molecular Sciences, 22(6), Article 2848. https://doi.org/10.3390/ijms22062848

Cas3 is a ssDNA-targeting nuclease-helicase essential for class 1 prokaryotic CRISPR immunity systems, which has been utilized for genome editing in human cells. Cas3-DNA crystal structures show that ssDNA follows a pathway from helicase domains into... Read More about A Tryptophan ‘Gate’ in the CRISPR-Cas3 Nuclease Controls ssDNA Entry into the Nuclease Site, That When Removed Results in Nuclease Hyperactivity.

The HelQ human DNA repair helicase utilizes a PWI-like domain for DNA loading through interaction with RPA, triggering DNA unwinding by the HelQ helicase core (2021)
Journal Article
Jenkins, T., Northall, S. J., Ptchelkine, D., Lever, R., Cubbon, A., Betts, H., …Bolt, E. L. (2021). The HelQ human DNA repair helicase utilizes a PWI-like domain for DNA loading through interaction with RPA, triggering DNA unwinding by the HelQ helicase core. NAR Cancer, 3(1), Article zcaa043. https://doi.org/10.1093/narcan/zcaa043

Genome instability is a characteristic enabling factor for carcinogenesis. HelQ helicase is a component of human DNA maintenance systems that prevent or reverse genome instability arising during DNA replication. Here, we provide details of the molecu... Read More about The HelQ human DNA repair helicase utilizes a PWI-like domain for DNA loading through interaction with RPA, triggering DNA unwinding by the HelQ helicase core.

Integration of diverse DNA substrates by a casposase can be targeted to R-loops in vitro by its fusion to Cas9 (2021)
Journal Article
Lau, C. H., & Bolt, E. L. (2021). Integration of diverse DNA substrates by a casposase can be targeted to R-loops in vitro by its fusion to Cas9. Bioscience Reports, 41(1), Article BSR20203595. https://doi.org/10.1042/bsr20203595

CRISPR systems build adaptive immunity against mobile genetic elements by DNA capture and integration catalysed by Cas1–Cas2 protein complexes. Recent studies suggested that CRISPR repeats and adaptation module originated from a novel type of DNA tra... Read More about Integration of diverse DNA substrates by a casposase can be targeted to R-loops in vitro by its fusion to Cas9.