αβDCA method identifies unspecific binding but specific disruption of the group I intron by the StpA chaperone.
RNA structure
StpA chaperone
direct coupling analysis
disordered protein
group I intron
Journal
RNA (New York, N.Y.)
ISSN: 1469-9001
Titre abrégé: RNA
Pays: United States
ID NLM: 9509184
Informations de publication
Date de publication:
11 2020
11 2020
Historique:
received:
12
12
2019
accepted:
19
07
2020
pubmed:
5
8
2020
medline:
23
1
2021
entrez:
5
8
2020
Statut:
ppublish
Résumé
Chaperone proteins-the most disordered among all protein groups-help RNAs fold into their functional structure by destabilizing misfolded configurations or stabilizing the functional ones. But disentangling the mechanism underlying RNA chaperoning is challenging, mostly because of inherent disorder of the chaperones and the transient nature of their interactions with RNA. In particular, it is unclear how specific the interactions are and what role is played by amino acid charge and polarity patterns. Here, we address these questions in the RNA chaperone StpA. We adapted direct coupling analysis (DCA) into the αβDCA method that can treat in tandem sequences written in two alphabets, nucleotides and amino acids. With αβDCA, we could analyze StpA-RNA interactions and show consistency with a previously proposed two-pronged mechanism: StpA disrupts
Identifiants
pubmed: 32747608
pii: rna.074336.119
doi: 10.1261/rna.074336.119
pmc: PMC7566574
doi:
Substances chimiques
DNA-Binding Proteins
0
Escherichia coli Proteins
0
Molecular Chaperones
0
StpA protein, E coli
0
RNA
63231-63-0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
1530-1540Informations de copyright
© 2020 Reinharz and Tlusty; Published by Cold Spring Harbor Laboratory Press for the RNA Society.
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