Protein-RNA complexation driven by the charge regulation mechanism.

Error message

Warning: A non-numeric value encountered in theme_biblio_tabular() (line 223 of /var/www/html/sites/all/modules/biblio/includes/
TitleProtein-RNA complexation driven by the charge regulation mechanism.
Publication TypeJournal Article
Year of Publication2017
Authorsda Silva FLuis Barro, Derreumaux P, Pasquali S
JournalBiochem Biophys Res Commun
Date Published2017 Jul 12

Electrostatic interactions play a pivotal role in many (bio)molecular association processes. The molecular organization and function in biological systems are largely determined by these interactions from pure Coulombic contributions to more peculiar mesoscopic forces due to ion-ion correlation and proton fluctuations. The latter is a general electrostatic mechanism that gives attraction particularly at low electrolyte concentrations. This charge regulation mechanism due to titrating amino acid and nucleotides residues is discussed here in a purely electrostatic framework. By means of constant-pH Monte Carlo simulations based on a fast coarse-grained titration proton scheme, a new computer molecular model was devised to study protein-RNA interactions. The complexation between the RNA silencing suppressor p19 viral protein and the 19-bp small interfering RNA was investigated at different solution pH and salt conditions. The outcomes illustrate the importance of the charge regulation mechanism that enhances the association between these macromolecules in a similar way as observed for other protein-polyelectrolyte systems typically found in colloidal science. Due to the highly negative charge of RNA, the effect is more pronounced in this system as predicted by the Kirkwood-Shumaker theory. Our results contribute to the general physico-chemical understanding of macromolecular complexation and shed light on the extensive role of RNA in the cell's life.

Alternate JournalBiochem. Biophys. Res. Commun.
Citation Key2017|2038
PubMed ID28709871