IFI16 Preferentially Binds to DNA with Quadruplex Structure and Enhances DNA Quadruplex Formation

0462078 - BFÚ 2017 RIV US eng J - Journal Article
Haroniková, Lucia - Coufal, Jan - Kejnovská, Iva - Jagelská, Eva - Fojta, Miroslav - Dvořáková, P. - Muller, P. - Vojtešek, B. - Brázda, Václav
IFI16 Preferentially Binds to DNA with Quadruplex Structure and Enhances DNA Quadruplex Formation.
PLoS ONE. Roč. 11, č. 6 (2016). ISSN 1932-6203. E-ISSN 1932-6203
R&D Projects: GA ČR GA15-21855S; GA ČR(CZ) GBP206/12/G151
Institutional support: RVO:68081707
Keywords : INTERFERON-INDUCIBLE PROTEIN * CIRCULAR-DICHROISM SPECTROSCOPY * RELEVANT G-QUADRUPLEX
Subject RIV: BO - Biophysics
Impact factor: 2.806, year: 2016

nterferon-inducible protein 16 (IFI16) is a member of the HIN-200 protein family, containing two HIN domains and one PYRIN domain. IFI16 acts as a sensor of viral and bacterial DNA and is important for innate immune responses. IFI16 binds DNA and binding has been described to be DNA length-dependent, but a preference for supercoiled DNA has also been demonstrated. Here we report a specific preference of IFI16 for binding to quadruplex DNA compared to other DNA structures. IFI16 binds to quadruplex DNA with significantly higher affinity than to the same sequence in double stranded DNA. By circular dichroism (CD) spectroscopy we also demonstrated the ability of IFI16 to stabilize quadruplex structures with quadruplex-forming oligonucleotides derived from human telomere (HTEL) sequences and the MYC promotor. A novel H/D exchange mass spectrometry approach was developed to assess protein interactions with quadruplex DNA.
Permanent Link: http://hdl.handle.net/11104/0261610