TY  - JOUR
A1  - Meiser, Nathalie
A1  - Fuks, Christin
A1  - Hengesbach, Martin
T1  - Cooperative analysis of structural dynamics in rna-protein complexes by single-molecule förster resonance energy transfer spectroscopy
T2  - Molecules
N2  - 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.
KW  - RNA-protein complex (RNP)
KW  - single-molecule förster resonance energy transfer (smFRET) spectroscopy
KW  - RNP dynamics
KW  - spliceosome
KW  - G quadruplex helicase RHAU
KW  - telomerase
Y1  - 2020
UR  - http://publikationen.ub.uni-frankfurt.de/frontdoor/index/index/docId/54435
UR  - https://nbn-resolving.org/urn:nbn:de:hebis:30:3-544355
SN  - 1420-3049
N1  - This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited
VL  - 25
IS  - 9, Art. 2057
SP  - 1
EP  - 19
PB  - MDPI
CY  - Basel
ER  -