Structural characterization of two prototypical repressors of SorC family reveals tetrameric assemblies on DNA and mechanism of function

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F24%3A00586786" target="_blank" >RIV/61388971:_____/24:00586786 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/61388963:_____/24:00586786 RIV/00216224:14740/24:00139056

Výsledek na webu

<a href="https://doi.org/10.1093/nar/gkae434" target="_blank" >https://doi.org/10.1093/nar/gkae434</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1093/nar/gkae434" target="_blank" >10.1093/nar/gkae434</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Structural characterization of two prototypical repressors of SorC family reveals tetrameric assemblies on DNA and mechanism of function

Popis výsledku v původním jazyce

The SorC family of transcriptional regulators plays a crucial role in controlling the carbohydrate metabolism and quorum sensing. We employed an integrative approach combining X-ray crystallography and cryo-electron microscopy to investigate architecture and functional mechanism of two prototypical representatives of two sub-classes of the SorC family: DeoR and CggR from Bacillus subtilis. Despite possessing distinct DNA-binding domains, both proteins form similar tetrameric assemblies when bound to their respective DNA operators. Structural analysis elucidates the process by which the CggR-regulated gapA operon is derepressed through the action of two effectors: fructose-1,6-bisphosphate and newly confirmed dihydroxyacetone phosphate. Our findings provide the first comprehensive understanding of the DNA binding mechanism of the SorC-family proteins, shedding new light on their functional characteristics.

Název v anglickém jazyce

Structural characterization of two prototypical repressors of SorC family reveals tetrameric assemblies on DNA and mechanism of function

Popis výsledku anglicky

The SorC family of transcriptional regulators plays a crucial role in controlling the carbohydrate metabolism and quorum sensing. We employed an integrative approach combining X-ray crystallography and cryo-electron microscopy to investigate architecture and functional mechanism of two prototypical representatives of two sub-classes of the SorC family: DeoR and CggR from Bacillus subtilis. Despite possessing distinct DNA-binding domains, both proteins form similar tetrameric assemblies when bound to their respective DNA operators. Structural analysis elucidates the process by which the CggR-regulated gapA operon is derepressed through the action of two effectors: fructose-1,6-bisphosphate and newly confirmed dihydroxyacetone phosphate. Our findings provide the first comprehensive understanding of the DNA binding mechanism of the SorC-family proteins, shedding new light on their functional characteristics.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10608 - Biochemistry and molecular biology

Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2024

Kód důvěrnosti údajů

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

Název periodika

Nucleic Acids Research

ISSN

0305-1048

e-ISSN

1362-4962

Svazek periodika

52

Číslo periodika v rámci svazku

12

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

16

Strana od-do

7305-7320

Kód UT WoS článku

001241820300001

EID výsledku v databázi Scopus

2-s2.0-85197970745