What the Hel: recent advances in understanding rifampicin resistance in bacteria
The result's identifiers
Result code in 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>
Alternative codes found
RIV/86652036:_____/23:00575356 RIV/61388971:_____/23:00575356
Result on the web
<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>
Alternative languages
Result language
angličtina
Original language name
What the Hel: recent advances in understanding rifampicin resistance in bacteria
Original language description
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.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10608 - Biochemistry and molecular biology
Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2023
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
FEMS Microbiology Reviews
ISSN
0168-6445
e-ISSN
1574-6976
Volume of the periodical
47
Issue of the periodical within the volume
6
Country of publishing house
US - UNITED STATES
Number of pages
9
Pages from-to
fuac051
UT code for WoS article
000912791800001
EID of the result in the Scopus database
2-s2.0-85180319909