ArticleACS omega2020
Recognition and Unfolding of c-MYC and Telomeric G-Quadruplex DNAs by the RecQ C-Terminal Domain of Human Bloom Syndrome Helicase.
Article in ACS omega, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
What it found
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Who cites it
4 citing papers in PubMed, 9 citations in OpenAlex.
- Functional role and folding properties of the glucan-binding domain of oral bacterial glucansucrase.FEBS letters · 2025Article
- Targeting RECQL4 in hepatocellular carcinoma: from prognosis to therapeutic potential.BMC medical genomics · 2025Article
- Unfolding of an RNA G-quadruplex motif in the negative strand genome of porcine reproductive and respiratory syndrome virus by host and viral helicases to promote viral replication.Nucleic acids research · 2023Article
- G-quadruplexes in bacteria: insights into the regulatory roles and interacting proteins of non-canonical nucleic acid structures.Critical reviews in biochemistry and molecular biologyReview
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
G-quadruplex (G4) is a noncanonical DNA secondary structure formed by Hoogsteen base pairing. It is recognized by various DNA helicases involved in DNA metabolism processes such as replication and transcription. Human Bloom syndrome protein (BLM), one of five human RecQ helicases, is a G4 helicase. While several studies revealed the mechanism of G4 binding and unfolding by the conserved RecQ C-terminal (RQC) domain of BLM, how RQC recognizes different G4 topologies is still unclear. Here, we investigated the interaction of Myc-22(14/23T) G4 from the c-Myc promoter and hTelo G4 from the telomeric sequence with RQC. Myc-22(14/23T) and hTelo form parallel and (3+1) hybrid topologies, respectively. Our circular dichroism (CD) spectroscopy data indicate that RQC can partially unfold the parallel G4, even with a short 3' overhang, while it can only partially unfold the (3+1) hybrid G4 with a 3' overhang of 6 nucleotides or longer. We found that the intrinsic thermal stability of G4 does not determine RQC-induced G4 unfolding by comparing
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Registered trials
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