The C-Terminal RRM/ACT Domain Is Crucial for Fine-Tuning the Activation of 'Long' RelA-SpoT Homolog Enzymes by Ribosomal Complexes.
ACT
RRM
Rel
ppGpp
ribosome
stringent response
Journal
Frontiers in microbiology
ISSN: 1664-302X
Titre abrégé: Front Microbiol
Pays: Switzerland
ID NLM: 101548977
Informations de publication
Date de publication:
2020
2020
Historique:
received:
21
11
2019
accepted:
06
02
2020
entrez:
19
3
2020
pubmed:
19
3
2020
medline:
19
3
2020
Statut:
epublish
Résumé
The (p)ppGpp-mediated stringent response is a bacterial stress response implicated in virulence and antibiotic tolerance. Both synthesis and degradation of the (p)ppGpp alarmone nucleotide are mediated by RelA-SpoT Homolog (RSH) enzymes which can be broadly divided in two classes: single-domain 'short' and multi-domain 'long' RSH. The regulatory ACT (Aspartokinase, Chorismate mutase and TyrA)/RRM (RNA Recognition Motif) domain is a near-universal C-terminal domain of long RSHs. Deletion of RRM in both monofunctional (synthesis-only) RelA as well as bifunctional (i.e., capable of both degrading and synthesizing the alarmone) Rel renders the long RSH cytotoxic due to overproduction of (p)ppGpp. To probe the molecular mechanism underlying this effect we characterized
Identifiants
pubmed: 32184768
doi: 10.3389/fmicb.2020.00277
pmc: PMC7058999
doi:
Types de publication
Journal Article
Langues
eng
Pagination
277Informations de copyright
Copyright © 2020 Takada, Roghanian, Murina, Dzhygyr, Murayama, Akanuma, Atkinson, Garcia-Pino and Hauryliuk.
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