Cooperative Analysis of Structural Dynamics in RNA-Protein Complexes by Single-Molecule Förster Resonance Energy Transfer Spectroscopy.
Animals
Cattle
Cluster Analysis
Crystallography, X-Ray
Fluorescence Resonance Energy Transfer
G-Quadruplexes
Humans
Markov Chains
Nucleic Acid Conformation
Protein Binding
Protein Denaturation
Protein Folding
Protein Structure, Secondary
RNA
/ chemistry
RNA Splicing
Ribonucleoproteins
Single Molecule Imaging
Spliceosomes
/ chemistry
Telomerase
/ chemistry
Telomere
/ chemistry
G quadruplex helicase RHAU
RNA-protein complex (RNP)
RNP dynamics
single-molecule förster resonance energy transfer (smFRET) spectroscopy
spliceosome
telomerase
Journal
Molecules (Basel, Switzerland)
ISSN: 1420-3049
Titre abrégé: Molecules
Pays: Switzerland
ID NLM: 100964009
Informations de publication
Date de publication:
28 Apr 2020
28 Apr 2020
Historique:
received:
25
02
2020
revised:
31
03
2020
accepted:
13
04
2020
entrez:
2
5
2020
pubmed:
2
5
2020
medline:
26
2
2021
Statut:
epublish
Résumé
RNA-protein complexes (RNPs) are essential components in a variety of cellular processes, and oftentimes exhibit complex structures and show mechanisms that are highly dynamic in conformation and structure. However, biochemical and structural biology approaches are mostly not able to fully elucidate the structurally and especially conformationally dynamic and heterogeneous nature of these RNPs, to which end single molecule Förster resonance energy transfer (smFRET) spectroscopy can be harnessed to fill this gap. Here we summarize the advantages of strategic smFRET studies to investigate RNP dynamics, complemented by structural and biochemical data. Focusing on recent smFRET studies of three essential biological systems, we demonstrate that investigation of RNPs on a single molecule level can answer important functional questions that remained elusive with structural or biochemical approaches alone: The complex structural rearrangements throughout the splicing cycle, unwinding dynamics of the G-quadruplex (G4) helicase RHAU, and aspects in telomere maintenance regulation and synthesis.
Identifiants
pubmed: 32354083
pii: molecules25092057
doi: 10.3390/molecules25092057
pmc: PMC7248720
pii:
doi:
Substances chimiques
Ribonucleoproteins
0
RNA
63231-63-0
Telomerase
EC 2.7.7.49
Types de publication
Journal Article
Review
Langues
eng
Sous-ensembles de citation
IM
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