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

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F68081707%3A_____%2F23%3A00574524" target="_blank" >RIV/68081707:_____/23:00574524 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/00216224:14310/23:00131002 RIV/00216305:26310/23:PU149606 RIV/00209805:_____/23:00079309

Výsledek na webu

<a href="https://www.sciencedirect.com/science/article/pii/S0006291X23006125?via%3Dihub" target="_blank" >https://www.sciencedirect.com/science/article/pii/S0006291X23006125?via%3Dihub</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.bbrc.2023.05.049" target="_blank" >10.1016/j.bbrc.2023.05.049</a>

Jazyk výsledku

angličtina

Název v původním jazyce

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

Popis výsledku v původním jazyce

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.

Název v anglickém jazyce

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

Popis výsledku anglicky

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.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

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OECD FORD obor

10608 - Biochemistry and molecular biology

Projekt

<a href="/cs/project/GA22-21903S" target="_blank" >GA22-21903S: Lokální struktury DNA a jejich role ve funkci mutantního proteinu p53 z lidských nádorů</a><br>

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2023

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Biochemical and Biophysical Research Communications

ISSN

0006-291X

e-ISSN

1090-2104

Svazek periodika

667

Číslo periodika v rámci svazku

JUL 30 2023

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

6

Strana od-do

89-94

Kód UT WoS článku

001001487800001

EID výsledku v databázi Scopus

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