Abstract:
In bacteria, transcription, translation and gene regulation are highly coupled processes. The achievement of a certain functional structure at a distinct temporal and spatial position is therefore essential for RNA molecules. Proteins that facilitate this proper folding of RNA molecules are called RNA chaperones. Here a prominent example from E. coli is reviewed: the nucleoid associated protein StpA. Based on its various RNA remodeling functions, we propose a mechanistic model that explains how StpA promotes RNA folding. Through transient interactions via the RNA backbone, thereby shielding repelling charges in RNA, it pre-positions the RNA molecules for the successful formation of transition states from encounter complexes.
Martina Doetsch,
Thomas Gstrein,
Renée Schroeder,
*Boris Fürtig
Pages 735 - 743
Downloads
Article PDF
Sharing
Email Page
Print Page
Share on Facebook
Share on Twitter
Share on LinkedIn
Related Articles