Dissecting Monomer-Dimer Equilibrium of an RNase P Protein Provides Insight Into the Synergistic Flexibility of 5' Leader Pre-tRNA Recognition.
RNA
binding
diffusion coefficient
folding
ribonuclease P
solution NMR
substrate recognition
tRNA processing
Journal
Frontiers in molecular biosciences
ISSN: 2296-889X
Titre abrégé: Front Mol Biosci
Pays: Switzerland
ID NLM: 101653173
Informations de publication
Date de publication:
2021
2021
Historique:
received:
24
06
2021
accepted:
18
08
2021
entrez:
20
9
2021
pubmed:
21
9
2021
medline:
21
9
2021
Statut:
epublish
Résumé
Ribonuclease P (RNase P) is a universal RNA-protein endonuclease that catalyzes 5' precursor-tRNA (ptRNA) processing. The RNase P RNA plays the catalytic role in ptRNA processing; however, the RNase P protein is required for catalysis
Identifiants
pubmed: 34540901
doi: 10.3389/fmolb.2021.730274
pii: 730274
pmc: PMC8447495
doi:
Types de publication
Journal Article
Langues
eng
Pagination
730274Subventions
Organisme : NIGMS NIH HHS
ID : R01 GM120572
Pays : United States
Organisme : NIH HHS
ID : S10 OD025000
Pays : United States
Organisme : NIGMS NIH HHS
ID : T32 GM007347
Pays : United States
Informations de copyright
Copyright © 2021 Zeng, Abzhanova, Brown and Reiter.
Déclaration de conflit d'intérêts
The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest.
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