Dual mode of IFI16 binding to supercoiled and linear DNA: A closer insight

0574524 - BFÚ 2024 RIV US eng J - Journal Article
Valková, Natalia - Kratochvilova, L. - Martinková, L. - Brázda, Václav
Dual mode of IFI16 binding to supercoiled and linear DNA: A closer insight.
Biochemical and Biophysical Research Communications. Roč. 667, JUL 30 2023 (2023), s. 89-94. ISSN 0006-291X. E-ISSN 1090-2104
R&D Projects: GA ČR(CZ) GA22-21903S
Institutional support: RVO:68081707
Keywords : ifi16 * Superhelicity * dna * afm * G-quadruplex * Inverted repeat
OECD category: Biochemistry and molecular biology
Impact factor: 3.1, year: 2022
Method of publishing: Limited access
https://www.sciencedirect.com/science/article/pii/S0006291X23006125?via%3Dihub

IFI16 (Interferon inducible protein 16) is a DNA sensor responsible for innate immune response stimu-lation and a direct viral restriction by modulating gene expression and replication. Many IFI16-DNA binding properties were describedlength-dependent and sequence-independent binding, oligomeri-zation of IFI16 upon recognition, sliding on the DNA, and preference for supercoiled DNA. However, the question of the role of IFI16-DNA binding in distinct IFI16 functions remains unclear. Here we demon-strate two modes of IFI16 binding to DNA using atomic force microscopy and electrophoretic mobility shift assays. In our study, we show that IFI16 can bind to DNA in the form of globular complexes or oligomers depending on DNA topology and molar ratios. The stability of the complexes is different in higher salt concentrations. In addition, we observed no preferential binding with the HIN-A or HIN-B domains to supercoiled DNA, revealing the importance of the whole protein for this specificity. These results provide more profound insight into IFI16-DNA interactions and may be important in answering the question of self-and non-self-DNA binding by the IFI16 protein and potentially could shed light on the role of DNA binding in distinct IFI16 functions.(c) 2023 Elsevier Inc. All rights reserved.
Permanent Link: https://hdl.handle.net/11104/0349252