What the Hel: recent advances in understanding rifampicin resistance in bacteria
Identifikátory výsledku
Kód výsledku v IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F23%3A00575356" target="_blank" >RIV/61388963:_____/23:00575356 - isvavai.cz</a>
Nalezeny alternativní kódy
RIV/86652036:_____/23:00575356 RIV/61388971:_____/23:00575356
Výsledek na webu
<a href="https://academic.oup.com/femsre/advance-article/doi/10.1093/femsre/fuac051/6957393?login=true" target="_blank" >https://academic.oup.com/femsre/advance-article/doi/10.1093/femsre/fuac051/6957393?login=true</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1093/femsre/fuac051" target="_blank" >10.1093/femsre/fuac051</a>
Alternativní jazyky
Jazyk výsledku
angličtina
Název v původním jazyce
What the Hel: recent advances in understanding rifampicin resistance in bacteria
Popis výsledku v původním jazyce
Rifampicin is a clinically important antibiotic that binds to, and blocks the DNA/RNA channel of bacterial RNA polymerase (RNAP). Stalled, nonfunctional RNAPs can be removed from DNA by HelD proteins, this is important for maintenance of genome integrity. Recently, it was reported that HelD proteins from high G+C Actinobacteria, called HelR, are able to dissociate rifampicin-stalled RNAPs from DNA and provide rifampicin resistance. This is achieved by the ability of HelR proteins to dissociate rifampicin from RNAP. The HelR-mediated mechanism of rifampicin resistance is discussed here, and the roles of HelD/HelR in the transcriptional cycle are outlined. Moreover, the possibility that the structurally similar HelD proteins from low G+C Firmicutes may be also involved in rifampicin resistance is explored. Finally, the discovery of the involvement of HelR in rifampicin resistance provides a blueprint for analogous studies to reveal novel mechanisms of bacterial antibiotic resistance.
Název v anglickém jazyce
What the Hel: recent advances in understanding rifampicin resistance in bacteria
Popis výsledku anglicky
Rifampicin is a clinically important antibiotic that binds to, and blocks the DNA/RNA channel of bacterial RNA polymerase (RNAP). Stalled, nonfunctional RNAPs can be removed from DNA by HelD proteins, this is important for maintenance of genome integrity. Recently, it was reported that HelD proteins from high G+C Actinobacteria, called HelR, are able to dissociate rifampicin-stalled RNAPs from DNA and provide rifampicin resistance. This is achieved by the ability of HelR proteins to dissociate rifampicin from RNAP. The HelR-mediated mechanism of rifampicin resistance is discussed here, and the roles of HelD/HelR in the transcriptional cycle are outlined. Moreover, the possibility that the structurally similar HelD proteins from low G+C Firmicutes may be also involved in rifampicin resistance is explored. Finally, the discovery of the involvement of HelR in rifampicin resistance provides a blueprint for analogous studies to reveal novel mechanisms of bacterial antibiotic resistance.
Klasifikace
Druh
J<sub>imp</sub> - Článek v periodiku v databázi Web of Science
CEP obor
—
OECD FORD obor
10608 - Biochemistry and molecular biology
Návaznosti výsledku
Projekt
Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.
Návaznosti
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Ostatní
Rok uplatnění
2023
Kód důvěrnosti údajů
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Údaje specifické pro druh výsledku
Název periodika
FEMS Microbiology Reviews
ISSN
0168-6445
e-ISSN
1574-6976
Svazek periodika
47
Číslo periodika v rámci svazku
6
Stát vydavatele periodika
US - Spojené státy americké
Počet stran výsledku
9
Strana od-do
fuac051
Kód UT WoS článku
000912791800001
EID výsledku v databázi Scopus
2-s2.0-85180319909