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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 str uct ures and organizing ribonucleoprotein comple x es. In our study, w e conducted a systematic analysis of the helicase-related activities of Esc heric hia coli HrpA and presented the str uct ures of both its apo form and its complex bound with both conventional and non-canonical DNAs. Our findings reveal that HrpA exhibits NTP h y droly sis activity and binds to ssDNA and ssRNA in distinct sequence-dependent manners. While the helicase core pla y s an essential role in unwinding RNA / RNA and RNA / DNA duple x es, the N-terminal e xtension in HrpA, consisting of three helices referred to as the APHB domain, is crucial for ssDNA binding and RNA / DNA duple x un winding. Import antly, the APHB domain is implicated in binding to non-canonical DNA str uct ures such as G-quadruplex and i-motif, and this report presents the first solved i-motif-helicase comple x. T his research not only provides comprehensive insights into the multifaceted roles of HrpA as an RNA helicase but also establishes a f oundation f or further in v estigations into the recognition and functional implications of i-motif DNA str uct ures in various biological processes. Gr aphical abstr act
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Dates et versions

hal-04472793 , version 1 (22-02-2024)

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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, In press, ⟨10.1093/nar/gkae138⟩. ⟨hal-04472793⟩
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