A nucleotide-switch mechanism mediates opposing catalytic activities of Rel enzymes.
Amino Acid Sequence
Bacteria
/ metabolism
Bacterial Proteins
/ metabolism
Catalytic Domain
Gene Expression Regulation, Bacterial
/ genetics
Genes, rel
/ genetics
Guanosine Pentaphosphate
/ metabolism
Guanosine Tetraphosphate
/ metabolism
Hydrolases
/ metabolism
Ligases
/ metabolism
Nucleotides
/ metabolism
Proto-Oncogene Proteins c-rel
/ genetics
Ribosomes
/ metabolism
Thermus thermophilus
/ enzymology
Journal
Nature chemical biology
ISSN: 1552-4469
Titre abrégé: Nat Chem Biol
Pays: United States
ID NLM: 101231976
Informations de publication
Date de publication:
08 2020
08 2020
Historique:
received:
22
06
2019
accepted:
13
03
2020
pubmed:
13
5
2020
medline:
24
11
2020
entrez:
13
5
2020
Statut:
ppublish
Résumé
Bifunctional Rel stringent factors, the most abundant class of RelA/SpoT homologs, are ribosome-associated enzymes that transfer a pyrophosphate from ATP onto the 3' of guanosine tri-/diphosphate (GTP/GDP) to synthesize the bacterial alarmone (p)ppGpp, and also catalyze the 3' pyrophosphate hydrolysis to degrade it. The regulation of the opposing activities of Rel enzymes is a complex allosteric mechanism that remains an active research topic despite decades of research. We show that a guanine-nucleotide-switch mechanism controls catalysis by Thermus thermophilus Rel (Rel
Identifiants
pubmed: 32393900
doi: 10.1038/s41589-020-0520-2
pii: 10.1038/s41589-020-0520-2
doi:
Substances chimiques
Bacterial Proteins
0
Nucleotides
0
Proto-Oncogene Proteins c-rel
0
Guanosine Tetraphosphate
33503-72-9
Guanosine Pentaphosphate
38918-96-6
Hydrolases
EC 3.-
Ligases
EC 6.-
guanosine 3',5'-polyphosphate synthetases
EC 6.-
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
834-840Références
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