This title appears in the Scientific Report :
2021
Please use the identifier:
http://dx.doi.org/10.1128/JVI.01505-20 in citations.
Please use the identifier: http://hdl.handle.net/2128/27932 in citations.
Biophysical and Dynamic Characterization of Fine-Tuned Binding of the Human Respiratory Syncytial Virus M2-1 Core Domain to Long RNAs
Biophysical and Dynamic Characterization of Fine-Tuned Binding of the Human Respiratory Syncytial Virus M2-1 Core Domain to Long RNAs
The human respiratory syncytial virus (hRSV) M2-1 protein functions as a processivity and antitermination factor of the viral polymerase complex. Here, the first evidence that the hRSV M2-1 core domain (cdM2-1) alone has an unfolding activity for long RNAs is presented and the biophysical and dynami...
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Personal Name(s): | Caruso, Icaro P. |
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Guimarães, Giovana C. / Machado, Vitor B. / Fossey, Marcelo A. / Willbold, Dieter / Almeida, Fabio C. L. / Souza, Fátima P. (Corresponding author) | |
Contributing Institute: |
Strukturbiochemie; IBI-7 |
Published in: | Journal of virology, 94 (2020) 23, S. e01505-20 |
Imprint: |
Baltimore, Md.
Soc.
2020
|
DOI: |
10.1128/JVI.01505-20 |
Document Type: |
Journal Article |
Research Program: |
Physical Basis of Diseases |
Link: |
Published on 2020-11-09. Available in OpenAccess from 2021-05-09. Get full text |
Publikationsportal JuSER |
Please use the identifier: http://hdl.handle.net/2128/27932 in citations.
The human respiratory syncytial virus (hRSV) M2-1 protein functions as a processivity and antitermination factor of the viral polymerase complex. Here, the first evidence that the hRSV M2-1 core domain (cdM2-1) alone has an unfolding activity for long RNAs is presented and the biophysical and dynamic characterization of the cdM2-1/RNA complex is provided. The main contact region of cdM2-1 with RNA was the α1-α2-α5-α6 helix bundle, which suffered local conformational changes and promoted the RNA unfolding activity. This activity may be triggered by base-pairing recognition. RNA molecules wrap around the whole cdM2-1, protruding their termini over the domain. The α2-α3 and α3-α4 loops of cdM2-1 were marked by an increase in picosecond internal motions upon RNA binding, even though they are not directly involved in the interaction. The results revealed that the cdM2-1/RNA complex originates from a fine-tuned binding, contributing to the unraveling interaction aspects necessary for M2-1 activity. |