Article Dans Une Revue Nucleic Acids Research Année : 2024

Structural insights into the N-terminal APHB domain of HrpA: mediating canonical and i-motif recognition

Résumé

RNA helicases function as versatile enzymes primarily responsible for remodeling RNA secondary structures and organizing ribonucleoprotein complexes. In our study, we conducted a systematic analysis of the helicase-related activities of Escherichia coli HrpA and presented the structures of both its apo form and its complex bound with both conventional and non-canonical DNAs. Our findings reveal that HrpA exhibits NTP hydrolysis activity and binds to ssDNA and ssRNA in distinct sequence-dependent manners. While the helicase core plays an essential role in unwinding RNA/RNA and RNA/DNA duplexes, the N-terminal extension in HrpA, consisting of three helices referred to as the APHB domain, is crucial for ssDNA binding and RNA/DNA duplex unwinding. Importantly, the APHB domain is implicated in binding to non-canonical DNA structures such as G-quadruplex and i-motif, and this report presents the first solved i-motif-helicase complex. This research not only provides comprehensive insights into the multifaceted roles of HrpA as an RNA helicase but also establishes a foundation for further investigations into the recognition and functional implications of i-motif DNA structures in various biological processes.
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hal-04730219 , version 1 (10-10-2024)

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Ben-Ge Xin, Ling-Yun Huang, Ling-Gang Yuan, Na-Nv Liu, Hai-Hong Li, et al.. Structural insights into the N-terminal APHB domain of HrpA: mediating canonical and i-motif recognition. Nucleic Acids Research, 2024, 52 (6), pp.3406-3418. ⟨10.1093/nar/gkae138⟩. ⟨hal-04730219⟩
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