The human Dicer helicase domain is capable of ATP hydrolysis and single-stranded nucleic acid binding
Preservation of ATPase activity by hDicer suggests that this enzyme performs many more functions in the cell than is currently assumed. Our findings open new avenues for future studies aimed at defining the cellular activities of hDicer that may be associated with these newly described biochemical properties: ATP hydrolysis and single-stranded nucleic acid binding activities.
Authors
- Kamil Szpotkowski (ORCID: https://orcid.org/0000-0002-7101-7200)
- Klaudia Wójcik (ORCID: https://orcid.org/0000-0003-3719-0795)
- Agnieszka Szczepańska (ORCID: https://orcid.org/0000-0001-8548-4099)
- Anna Kurzyńska‐Kokorniak (ORCID: https://orcid.org/0000-0002-7034-3370)
- Anna Urbanowicz (ORCID: https://orcid.org/0000-0002-6854-7737)
- Kinga Ciechanowska (ORCID: https://orcid.org/0000-0003-1958-0546)
Institutions
- Institute of Bioorganic Chemistry, Polish Academy of Sciences (PL)
Publication Details
- Journal
- BMC Biology
- Published
- 2024-12-18
- DOI
- https://doi.org/10.1186/s12915-024-02082-x
- Citations
- 3
- Primary Topic
- Plant Virus Research Studies
- Type
- article
- Field-Weighted Citation Impact
- 1.80
Funders
- Deutsches Elektronen-Synchrotron