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

J 2024

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

SOLTYSOVA, Marketa; Jana SKERLOVA; Petr PACHL; Karel ŠKUBNÍK; Milan FABRY et. al.

Základní údaje

Originální název

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

Autoři

SOLTYSOVA, Marketa; Jana SKERLOVA; Petr PACHL; Karel ŠKUBNÍK; Milan FABRY; Irena SIEGLOVA; Martina FAROLFI; Irina GRISHKOVSKAYA; Michal BABIAK; Jiří NOVÁČEK; Libor KRASNY a Pavlina REZACOVA

Vydání

Nucleic acids research, Oxford, Oxford University Press, 2024, 0305-1048

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10608 Biochemistry and molecular biology

Stát vydavatele

Velká Británie a Severní Irsko

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 13.100

Kód RIV

RIV/00216224:14740/24:00139056

Organizační jednotka

Středoevropský technologický institut

DOI

https://doi.org/10.1093/nar/gkae434

UT WoS

001241820300001

EID Scopus

2-s2.0-85197970745

Klíčová slova anglicky

CENTRAL GLYCOLYTIC GENES; EFFECTOR-BINDING DOMAIN; SUBTILIS RNA-POLYMERASE; NUPC-PDP OPERON; BACILLUS-SUBTILIS; TRANSCRIPTIONAL REGULATION; KLEBSIELLA-PNEUMONIAE; CRYSTAL-STRUCTURES; DEOR REPRESSOR; CCP4 SUITE

Štítky

CF CRYO, rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 14. 3. 2025 15:53, Mgr. Eva Dubská

Anotace

V originále

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.

Návaznosti

EF18_046/0015974, projekt VaV

Název: Modernizace České infrastruktury pro integrativní strukturní biologii

EH22_008/0004575, projekt VaV

Název: RNA pro terapii

LX22NPO5103, projekt VaV

Název: Národní institut virologie a bakteriologie (Akronym: NIVB)

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, Národní institut virologie a bakteriologie, 5.1 EXCELES

90242, velká výzkumná infrastruktura

Název: CIISB III

Citovat

SOLTYSOVA, Marketa; Jana SKERLOVA; Petr PACHL; Karel ŠKUBNÍK; Milan FABRY; Irena SIEGLOVA; Martina FAROLFI; Irina GRISHKOVSKAYA; Michal BABIAK; Jiří NOVÁČEK; Libor KRASNY a Pavlina REZACOVA. Structural characterization of two prototypical repressors of SorC family reveals tetrameric assemblies on DNA and mechanism of function. Nucleic acids research. Oxford: Oxford University Press, 2024, roč. 52, č. 12, s. 7305-7320. ISSN 0305-1048. Dostupné z: https://doi.org/10.1093/nar/gkae434.

@article{2483877,
   author = {Soltysova, Marketa and Skerlova, Jana and Pachl, Petr and Škubník, Karel and Fabry, Milan and Sieglova, Irena and Farolfi, Martina and Grishkovskaya, Irina and Babiak, Michal and Nováček, Jiří and Krasny, Libor and Rezacova, Pavlina},
   article_location = {Oxford},
   article_number = {12},
   doi = {https://doi.org/10.1093/nar/gkae434},
   keywords = {CENTRAL GLYCOLYTIC GENES; EFFECTOR-BINDING DOMAIN; SUBTILIS RNA-POLYMERASE; NUPC-PDP OPERON; BACILLUS-SUBTILIS; TRANSCRIPTIONAL REGULATION; KLEBSIELLA-PNEUMONIAE; CRYSTAL-STRUCTURES; DEOR REPRESSOR; CCP4 SUITE},
   language = {eng},
   issn = {0305-1048},
   journal = {Nucleic acids research},
   title = {Structural characterization of two prototypical repressors of SorC family reveals tetrameric assemblies on DNA and mechanism of function},
   url = {https://academic.oup.com/nar/article/52/12/7305/7688987?login=true},
   volume = {52},
   year = {2024}
}

TY  - JOUR
ID  - 2483877
AU  - Soltysova, Marketa - Skerlova, Jana - Pachl, Petr - Škubník, Karel - Fabry, Milan - Sieglova, Irena - Farolfi, Martina - Grishkovskaya, Irina - Babiak, Michal - Nováček, Jiří - Krasny, Libor - Rezacova, Pavlina
PY  - 2024
TI  - Structural characterization of two prototypical repressors of SorC family reveals tetrameric assemblies on DNA and mechanism of function
JF  - Nucleic acids research
VL  - 52
IS  - 12
SP  - 7305-7320
EP  - 7305-7320
PB  - Oxford University Press
SN  - 03051048
KW  - CENTRAL GLYCOLYTIC GENES
KW  - EFFECTOR-BINDING DOMAIN
KW  - SUBTILIS RNA-POLYMERASE
KW  - NUPC-PDP OPERON
KW  - BACILLUS-SUBTILIS
KW  - TRANSCRIPTIONAL REGULATION
KW  - KLEBSIELLA-PNEUMONIAE
KW  - CRYSTAL-STRUCTURES
KW  - DEOR REPRESSOR
KW  - CCP4 SUITE
UR  - https://academic.oup.com/nar/article/52/12/7305/7688987?login=true
N2  - 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.
ER  -

SOLTYSOVA, Marketa; Jana SKERLOVA; Petr PACHL; Karel ŠKUBNÍK; Milan FABRY; Irena SIEGLOVA; Martina FAROLFI; Irina GRISHKOVSKAYA; Michal BABIAK; Jiří NOVÁČEK; Libor KRASNY a Pavlina REZACOVA. Structural characterization of two prototypical repressors of SorC family reveals tetrameric assemblies on DNA and mechanism of function. \textit{Nucleic acids research}. Oxford: Oxford University Press, 2024, roč.~52, č.~12, s.~7305-7320. ISSN~0305-1048. Dostupné z: https://doi.org/10.1093/nar/gkae434.

Přehled o publikaci