Binding of the bacteriophage P22 N-peptide to the boxB RNA motif studied by molecular dynamics simulations

Ranjit P. Bahadur, Srinivasaraghavan Kannan, Martin Zacharias

Publikation: Beitrag in FachzeitschriftArtikelBegutachtung

29 Zitate (Scopus)

Abstract

Protein-RNA interactions are important for many cellular processes. The Nut-utilization site (N)-protein of bacteriophages contains an N-terminal arginine-rich motif that undergoes a folding transition upon binding to the boxB RNA hairpin loop target structure. Molecular dynamics simulations were used to investigate the dynamics of the P22 N-peptide-boxB complex and to elucidate the energetic contributions to binding. In addition, the free-energy changes of RNA and peptide conformational adaptation to the bound forms, as well as the role of strongly bound water molecules at the peptide-RNA interface, were studied. The influence of peptide amino acid substitutions and the salt dependence of interaction were investigated and showed good agreement with available experimental results. Several tightly bound water molecules were found at the RNA-binding interface in both the presence and absence of N-peptide. Explicit consideration of the waters resulted in shifts of calculated contributions during the energetic analysis, but overall similar binding energy contributions were found. Of interest, it was found that the electrostatic field of the RNA has a favorable influence on the coil-to-α-helix transition of the N-peptide already outside of the peptidebinding site. This result may have important implications for understanding peptide-RNA complex formation, which often involves coupled folding and association processes. It indicates that electrostatic interactions near RNA molecules can lead to a shift in the equilibrium toward the bound form of an interacting partner before it enters the binding pocket.

OriginalspracheEnglisch
Seiten (von - bis)3139-3149
Seitenumfang11
FachzeitschriftBiophysical Journal
Jahrgang97
Ausgabenummer12
DOIs
PublikationsstatusVeröffentlicht - 16 Dez. 2009
Extern publiziertJa

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