Factor-specific effects of mutations in the active site of RNA polymerase on RNA cleavage.
Gre factors
RNA polymerase
RNA proofreading
Transcription fidelity
Journal
Biochemical and biophysical research communications
ISSN: 1090-2104
Titre abrégé: Biochem Biophys Res Commun
Pays: United States
ID NLM: 0372516
Informations de publication
Date de publication:
26 02 2020
26 02 2020
Historique:
received:
26
11
2019
accepted:
07
12
2019
pubmed:
16
12
2019
medline:
17
9
2020
entrez:
16
12
2019
Statut:
ppublish
Résumé
Bacterial RNA polymerase (RNAP) relies on the same active site for RNA synthesis and co-transcriptional RNA proofreading. The intrinsic RNA proofreading activity of RNAP can be greatly stimulated by Gre factors, which bind within the secondary channel and directly participate in the RNA cleavage reaction in the active site of RNAP. Here, we characterize mutations in Escherichia coli RNAP that differentially affect intrinsic and Gre-stimulated RNA cleavage. Substitution of a highly conserved arginine residue that contacts nascent RNA upstream of the active site strongly impairs intrinsic and GreA-dependent cleavage, without reducing GreA affinity or catalytic Mg
Identifiants
pubmed: 31837805
pii: S0006-291X(19)32365-4
doi: 10.1016/j.bbrc.2019.12.045
pii:
doi:
Substances chimiques
Escherichia coli Proteins
0
DNA-Directed RNA Polymerases
EC 2.7.7.6
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
165-170Informations de copyright
Copyright © 2019 Elsevier Inc. All rights reserved.