Cooperative Analysis of Structural Dynamics in RNA-Protein Complexes by Single-Molecule Förster Resonance Energy Transfer Spectroscopy
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...
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| Format: | Article |
| Language: | English |
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MDPI AG
2020-04-01
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| Series: | Molecules |
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| Online Access: | https://www.mdpi.com/1420-3049/25/9/2057 |
| _version_ | 1797569401418940416 |
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| author | Nathalie Meiser Christin Fuks Martin Hengesbach |
| author_facet | Nathalie Meiser Christin Fuks Martin Hengesbach |
| author_sort | Nathalie Meiser |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-03-10T20:10:17Z |
| format | Article |
| id | doaj.art-31ed76cc637b437290187f8abac1c328 |
| institution | Directory Open Access Journal |
| issn | 1420-3049 |
| language | English |
| last_indexed | 2024-03-10T20:10:17Z |
| publishDate | 2020-04-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Molecules |
| spelling | doaj.art-31ed76cc637b437290187f8abac1c3282023-11-19T22:57:17ZengMDPI AGMolecules1420-30492020-04-01259205710.3390/molecules25092057Cooperative Analysis of Structural Dynamics in RNA-Protein Complexes by Single-Molecule Förster Resonance Energy Transfer SpectroscopyNathalie Meiser0Christin Fuks1Martin Hengesbach2Institute for Organic Chemistry and Chemical Biology, Goethe-University Frankfurt, Max-von-Laue-Str. 7, 60438 Frankfurt, GermanyInstitute for Organic Chemistry and Chemical Biology, Goethe-University Frankfurt, Max-von-Laue-Str. 7, 60438 Frankfurt, GermanyInstitute for Organic Chemistry and Chemical Biology, Goethe-University Frankfurt, Max-von-Laue-Str. 7, 60438 Frankfurt, GermanyRNA-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.https://www.mdpi.com/1420-3049/25/9/2057RNA-protein complex (RNP)single-molecule förster resonance energy transfer (smFRET) spectroscopyRNP dynamicsspliceosomeG quadruplex helicase RHAUtelomerase |
| spellingShingle | Nathalie Meiser Christin Fuks Martin Hengesbach Cooperative Analysis of Structural Dynamics in RNA-Protein Complexes by Single-Molecule Förster Resonance Energy Transfer Spectroscopy Molecules RNA-protein complex (RNP) single-molecule förster resonance energy transfer (smFRET) spectroscopy RNP dynamics spliceosome G quadruplex helicase RHAU telomerase |
| title | Cooperative Analysis of Structural Dynamics in RNA-Protein Complexes by Single-Molecule Förster Resonance Energy Transfer Spectroscopy |
| title_full | Cooperative Analysis of Structural Dynamics in RNA-Protein Complexes by Single-Molecule Förster Resonance Energy Transfer Spectroscopy |
| title_fullStr | Cooperative Analysis of Structural Dynamics in RNA-Protein Complexes by Single-Molecule Förster Resonance Energy Transfer Spectroscopy |
| title_full_unstemmed | Cooperative Analysis of Structural Dynamics in RNA-Protein Complexes by Single-Molecule Förster Resonance Energy Transfer Spectroscopy |
| title_short | Cooperative Analysis of Structural Dynamics in RNA-Protein Complexes by Single-Molecule Förster Resonance Energy Transfer Spectroscopy |
| title_sort | cooperative analysis of structural dynamics in rna protein complexes by single molecule forster resonance energy transfer spectroscopy |
| topic | RNA-protein complex (RNP) single-molecule förster resonance energy transfer (smFRET) spectroscopy RNP dynamics spliceosome G quadruplex helicase RHAU telomerase |
| url | https://www.mdpi.com/1420-3049/25/9/2057 |
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