Selection of RNA-Binding Peptides Using mRNA-Peptide Fusions

We have been working to apply in vitro selection to isolate novel RNA-binding peptides. To do this, we use mRNA-protein fusions, peptides covalently attached to their own mRNA. Here, we report selection protocols developed using the arginine-rich domain of bacteriophage lambda-N protein and its bind...

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Bibliographic Details
Published in:Methods (San Diego, Calif.) Calif.), 2001-03, Vol.23 (3), p.287-293
Main Authors: Barrick, Jeffrey E., Takahashi, Terry T., Balakin, Andrey, Roberts, Richard W.
Format: Article
Language:English
Subjects:
DNA, Complementary - metabolism
Genetic Techniques
in vitro selection
lambda-N
mRNA-peptide fusions
Peptides
Protein Biosynthesis
Protein Structure, Tertiary
Recombinant Fusion Proteins - metabolism
RNA, Messenger - metabolism
RNA-Binding Proteins - metabolism
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Summary:We have been working to apply in vitro selection to isolate novel RNA-binding peptides. To do this, we use mRNA-protein fusions, peptides covalently attached to their own mRNA. Here, we report selection protocols developed using the arginine-rich domain of bacteriophage lambda-N protein and its binding target, the boxB RNA. Systematic investigation of possible paths for a selection round has allowed us to design a reliable and efficient protocol to enrich RNA-binding peptides from nonfunctional members of a complex mixture. The protocols we have developed should greatly facilitate the isolation of new molecules using the fusion system.
ISSN:1046-2023
1095-9130
DOI:10.1006/meth.2000.1139