%0 Journal Article
%A Caruso, Icaro P.
%A Guimarães, Giovana C.
%A Machado, Vitor B.
%A Fossey, Marcelo A.
%A Willbold, Dieter
%A Almeida, Fabio C. L.
%A Souza, Fátima P.
%T Biophysical and Dynamic Characterization of Fine-Tuned Binding of the Human Respiratory Syncytial Virus M2-1 Core Domain to Long RNAs
%J Journal of virology
%V 94
%N 23
%@ 1098-5514
%C Baltimore, Md.
%I Soc.
%M FZJ-2021-00481
%P  e01505-20
%D 2020
%X 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.
%F PUB:(DE-HGF)16
%9 Journal Article
%$ 32938771
%U <Go to ISI:>//WOS:000595866900011
%R 10.1128/JVI.01505-20
%U https://juser.fz-juelich.de/record/889873