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

J 2023

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

VALKOVÁ, Natália, Libuše KRATOCHVILOVÁ, Lucia MARTINKOVÁ a Václav BRÁZDA

Základní údaje

Originální název

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

Autoři

VALKOVÁ, Natália (703 Slovensko, domácí), Libuše KRATOCHVILOVÁ, Lucia MARTINKOVÁ a Václav BRÁZDA (203 Česká republika, garant)

Vydání

Biochemical and Biophysical Research Communications, Elsevier B.V. 2023, 0006-291X

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10608 Biochemistry and molecular biology

Stát vydavatele

Spojené státy

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 2.500

Kód RIV

RIV/00216224:14310/23:00131002

Organizační jednotka

Přírodovědecká fakulta

DOI

http://dx.doi.org/10.1016/j.bbrc.2023.05.049

UT WoS

001001487800001

Klíčová slova anglicky

IFI16; Superhelicity; DNA; AFM; G-quadruplex; Inverted repeat

Štítky

rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 28. 6. 2023 14:05, Mgr. Marie Novosadová Šípková, DiS.

Anotace

V originále

IFI16 (Interferon inducible protein 16) is a DNA sensor responsible for innate immune response stimulation and a direct viral restriction by modulating gene expression and replication. Many IFI16-DNA binding properties were described - length-dependent and sequence-independent binding, oligomerization 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 demonstrate 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.

Citovat

VALKOVÁ, Natália, Libuše KRATOCHVILOVÁ, Lucia MARTINKOVÁ a Václav BRÁZDA. Dual mode of IFI16 binding to supercoiled and linear DNA: A closer insight. Biochemical and Biophysical Research Communications. Elsevier B.V., 2023, roč. 667, July, s. 89-94. ISSN 0006-291X. Dostupné z: https://dx.doi.org/10.1016/j.bbrc.2023.05.049.

@article{2292747,
   author = {Valková, Natália and Kratochvilová, Libuše and Martinková, Lucia and Brázda, Václav},
   article_number = {July},
   doi = {http://dx.doi.org/10.1016/j.bbrc.2023.05.049},
   keywords = {IFI16; Superhelicity; DNA; AFM; G-quadruplex; Inverted repeat},
   language = {eng},
   issn = {0006-291X},
   journal = {Biochemical and Biophysical Research Communications},
   title = {Dual mode of IFI16 binding to supercoiled and linear DNA: A closer insight},
   url = {https://doi.org/10.1016/j.bbrc.2023.05.049},
   volume = {667},
   year = {2023}
}

TY  - JOUR
ID  - 2292747
AU  - Valková, Natália - Kratochvilová, Libuše - Martinková, Lucia - Brázda, Václav
PY  - 2023
TI  - Dual mode of IFI16 binding to supercoiled and linear DNA: A closer insight
JF  - Biochemical and Biophysical Research Communications
VL  - 667
IS  - July
SP  - 89-94
EP  - 89-94
PB  - Elsevier B.V.
SN  - 0006291X
KW  - IFI16
KW  - Superhelicity
KW  - DNA
KW  - AFM
KW  - G-quadruplex
KW  - Inverted repeat
UR  - https://doi.org/10.1016/j.bbrc.2023.05.049
N2  - IFI16 (Interferon inducible protein 16) is a DNA sensor responsible for innate immune response stimulation and a direct viral restriction by modulating gene expression and replication. Many IFI16-DNA binding properties were described - length-dependent and sequence-independent binding, oligomerization 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 demonstrate 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.
ER  -

VALKOVÁ, Natália, Libuše KRATOCHVILOVÁ, Lucia MARTINKOVÁ a Václav BRÁZDA. Dual mode of IFI16 binding to supercoiled and linear DNA: A closer insight. \textit{Biochemical and Biophysical Research Communications}. Elsevier B.V., 2023, roč.~667, July, s.~89-94. ISSN~0006-291X. Dostupné z: https://dx.doi.org/10.1016/j.bbrc.2023.05.049.

Podrobný výpis o publikaci