RNase P Inhibitors Identified as Aggregators.
RNase P inhibitors
RnpA protein subunit
bacterial RNase P
protein aggregators
Journal
Antimicrobial agents and chemotherapy
ISSN: 1098-6596
Titre abrégé: Antimicrob Agents Chemother
Pays: United States
ID NLM: 0315061
Informations de publication
Date de publication:
16 07 2021
16 07 2021
Historique:
pubmed:
12
5
2021
medline:
10
8
2021
entrez:
11
5
2021
Statut:
ppublish
Résumé
RNase P is an essential enzyme responsible for tRNA 5'-end maturation. In most bacteria, the enzyme is a ribonucleoprotein consisting of a catalytic RNA subunit and a small protein cofactor termed RnpA. Several studies have reported small-molecule inhibitors directed against bacterial RNase P that were identified by high-throughput screenings. Using the bacterial RNase P enzymes from Thermotoga maritima, Bacillus subtilis, and Staphylococcus aureus as model systems, we found that such compounds, including RNPA2000 (and its derivatives), iriginol hexaacetate, and purpurin, induce the formation of insoluble aggregates of RnpA rather than acting as specific inhibitors. In the case of RNPA2000, aggregation was induced by Mg
Identifiants
pubmed: 33972249
pii: AAC.00300-21
doi: 10.1128/AAC.00300-21
pmc: PMC8284443
doi:
Substances chimiques
RNA, Bacterial
0
Ribonuclease P
EC 3.1.26.5
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
e0030021Références
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