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Structural mechanism of DNA recognition by the p204 HIN domain

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Structural mechanism of DNA recognition by the p204 HIN domain. / Fan, X.; Jiang, J.; Zhao, D. et al.
In: Nucleic Acids Research, Vol. 49, No. 5, 18.03.2021, p. 2959-2972.

Research output: Contribution to Journal/Magazine › Journal article › peer-review

Harvard

Fan, X, Jiang, J, Zhao, D, Chen, F, Ma, H, Smith, P, Unterholzner, L, Xiao, TS & Jin, T 2021, 'Structural mechanism of DNA recognition by the p204 HIN domain', Nucleic Acids Research, vol. 49, no. 5, pp. 2959-2972. https://doi.org/10.1093/nar/gkab076

APA

Fan, X., Jiang, J., Zhao, D., Chen, F., Ma, H., Smith, P., Unterholzner, L., Xiao, T. S., & Jin, T. (2021). Structural mechanism of DNA recognition by the p204 HIN domain. Nucleic Acids Research, 49(5), 2959-2972. https://doi.org/10.1093/nar/gkab076

Vancouver

Fan X, Jiang J, Zhao D, Chen F, Ma H, Smith P et al. Structural mechanism of DNA recognition by the p204 HIN domain. Nucleic Acids Research. 2021 Mar 18;49(5):2959-2972. Epub 2021 Feb 22. doi: 10.1093/nar/gkab076

Author

Fan, X. ; Jiang, J. ; Zhao, D. et al. / Structural mechanism of DNA recognition by the p204 HIN domain. In: Nucleic Acids Research. 2021 ; Vol. 49, No. 5. pp. 2959-2972.

Bibtex

@article{13d6499402d046fcac3e664286810c69,
title = "Structural mechanism of DNA recognition by the p204 HIN domain",
abstract = "The interferon gamma-inducible protein 16 (IFI16) and its murine homologous protein p204 function in non-sequence specific dsDNA sensing; however, the exact dsDNA recognition mechanisms of IFI16/p204, which harbour two HIN domains, remain unclear. In the present study, we determined crystal structures of p204 HINa and HINb domains, which are highly similar to those of other PYHIN family proteins. Moreover, we obtained the crystal structure of p204 HINab domain in complex with dsDNA and provided insights into the dsDNA binding mode. p204 HINab binds dsDNA mainly through α2 helix of HINa and HINb, and the linker between them, revealing a similar HIN:DNA binding mode. Both HINa and HINb are vital for HINab recognition of dsDNA, as confirmed by fluorescence polarization assays. Furthermore, a HINa dimerization interface was observed in structures of p204 HINa and HINab:dsDNA complex, which is involved in binding dsDNA. The linker between HINa and HINb reveals dynamic flexibility in solution and changes its direction at ∼90° angle in comparison with crystal structure of HINab:dsDNA complex. These structural information provide insights into the mechanism of DNA recognition by different HIN domains, and shed light on the unique roles of two HIN domains in activating the IFI16/p204 signaling pathway. ",
keywords = "DNA, Ifi16 protein, mouse, nuclear protein, phosphoprotein, protein binding, chemistry, metabolism, molecular model, protein domain, protein multimerization, X ray crystallography, Crystallography, X-Ray, Models, Molecular, Nuclear Proteins, Phosphoproteins, Protein Binding, Protein Domains, Protein Multimerization",
author = "X. Fan and J. Jiang and D. Zhao and F. Chen and H. Ma and P. Smith and L. Unterholzner and T.S. Xiao and T. Jin",
year = "2021",
month = mar,
day = "18",
doi = "10.1093/nar/gkab076",
language = "English",
volume = "49",
pages = "2959--2972",
journal = "Nucleic Acids Research",
issn = "0305-1048",
publisher = "Oxford University Press",
number = "5",

}

RIS

TY - JOUR

T1 - Structural mechanism of DNA recognition by the p204 HIN domain

AU - Fan, X.

AU - Jiang, J.

AU - Zhao, D.

AU - Chen, F.

AU - Ma, H.

AU - Smith, P.

AU - Unterholzner, L.

AU - Xiao, T.S.

AU - Jin, T.

PY - 2021/3/18

Y1 - 2021/3/18

N2 - The interferon gamma-inducible protein 16 (IFI16) and its murine homologous protein p204 function in non-sequence specific dsDNA sensing; however, the exact dsDNA recognition mechanisms of IFI16/p204, which harbour two HIN domains, remain unclear. In the present study, we determined crystal structures of p204 HINa and HINb domains, which are highly similar to those of other PYHIN family proteins. Moreover, we obtained the crystal structure of p204 HINab domain in complex with dsDNA and provided insights into the dsDNA binding mode. p204 HINab binds dsDNA mainly through α2 helix of HINa and HINb, and the linker between them, revealing a similar HIN:DNA binding mode. Both HINa and HINb are vital for HINab recognition of dsDNA, as confirmed by fluorescence polarization assays. Furthermore, a HINa dimerization interface was observed in structures of p204 HINa and HINab:dsDNA complex, which is involved in binding dsDNA. The linker between HINa and HINb reveals dynamic flexibility in solution and changes its direction at ∼90° angle in comparison with crystal structure of HINab:dsDNA complex. These structural information provide insights into the mechanism of DNA recognition by different HIN domains, and shed light on the unique roles of two HIN domains in activating the IFI16/p204 signaling pathway.

AB - The interferon gamma-inducible protein 16 (IFI16) and its murine homologous protein p204 function in non-sequence specific dsDNA sensing; however, the exact dsDNA recognition mechanisms of IFI16/p204, which harbour two HIN domains, remain unclear. In the present study, we determined crystal structures of p204 HINa and HINb domains, which are highly similar to those of other PYHIN family proteins. Moreover, we obtained the crystal structure of p204 HINab domain in complex with dsDNA and provided insights into the dsDNA binding mode. p204 HINab binds dsDNA mainly through α2 helix of HINa and HINb, and the linker between them, revealing a similar HIN:DNA binding mode. Both HINa and HINb are vital for HINab recognition of dsDNA, as confirmed by fluorescence polarization assays. Furthermore, a HINa dimerization interface was observed in structures of p204 HINa and HINab:dsDNA complex, which is involved in binding dsDNA. The linker between HINa and HINb reveals dynamic flexibility in solution and changes its direction at ∼90° angle in comparison with crystal structure of HINab:dsDNA complex. These structural information provide insights into the mechanism of DNA recognition by different HIN domains, and shed light on the unique roles of two HIN domains in activating the IFI16/p204 signaling pathway.

KW - DNA

KW - Ifi16 protein, mouse

KW - nuclear protein

KW - phosphoprotein

KW - protein binding

KW - chemistry

KW - metabolism

KW - molecular model

KW - protein domain

KW - protein multimerization

KW - X ray crystallography

KW - Crystallography, X-Ray

KW - Models, Molecular

KW - Nuclear Proteins

KW - Phosphoproteins

KW - Protein Binding

KW - Protein Domains

KW - Protein Multimerization

U2 - 10.1093/nar/gkab076

DO - 10.1093/nar/gkab076

M3 - Journal article

VL - 49

SP - 2959

EP - 2972

JO - Nucleic Acids Research

JF - Nucleic Acids Research

SN - 0305-1048

IS - 5

ER -