id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-278436-job4854r	Xie, Mao-Hua	A phage RNA-binding protein binds to a non-cognate structured RNA and stabilizes its core structure	2009-01-09		.txt	text/plain	3380	196	60	Recent studies suggest that some RNA-binding proteins facilitate the folding of non-cognate RNAs. Here, we report that bacteriophage MS2 coat protein (MS2 CP) bound and promoted the catalytic activity of Candida group I ribozyme. This mechanism is similar to that of the yeast mitochondrial tyrosyl-tRNA synthetase on other group I introns, suggesting that different RNA-binding proteins may use common mechanisms to support RNA structures. Interestingly, CYT 18 also stimulates the activity of several non-cognate group I introns [12] , questioning the specificity of the action of RNA-binding proteins. In this study, the protein-protected RNA cloning (PRC) method has been developed to successfully identify the MS2-binding site on the Candida group I ribozyme RNA. In summary, the finding of MS2 CP binding of the P5ab-P5 structure of the Candida group I ribozyme suggests that this phage protein can interact with a bulged RNA paired region connected to an asymmetric internal loop containing three adenines.	./cache/cord-278436-job4854r.txt	./txt/cord-278436-job4854r.txt