Specific RNA binding proteins constructed from zinc fingers
- 1 July 1998
- journal article
- Published by Springer Nature in Nature Structural & Molecular Biology
- Vol. 5 (7), 543-546
- https://doi.org/10.1038/794
Abstract
A zinc finger library with degenerate alpha-helices was displayed on the surface of bacteriophage and proteins that bind human immunodeficiency virus type-1 (HIV-1) Rev response element stem loop IIB (RRE-IIB) RNA or 5S rRNA were isolated. DNA encoding affinity selected zinc fingers was shuffled by recombination in vitro to isolate proteins with higher RNA binding affinity. Proteins constructed in this way bind RNA specifically both in vitro and in vivo. These results demonstrate that RNA substrate specificity of zinc fingers can be changed through mutation of alpha-helices to construct novel RNA binding proteins.Keywords
This publication has 22 references indexed in Scilit:
- Solution structure of the first three zinc fingers of TFIIIA bound to the cognate DNA sequence: determinants of affinity and sequence specificityJournal of Molecular Biology, 1997
- Phage Display of RNA Binding Zinc Fingers from Transcription Factor IIIAPublished by Elsevier ,1997
- Physical basis of a protein-DNA recognition codeCurrent Opinion in Structural Biology, 1997
- Selection of RNA-binding peptides in vivoNature, 1996
- A Molecular RheostatJournal of Molecular Biology, 1994
- RNA recognition by an isolated α helixCell, 1993
- Molecular Basis for Specific Recognition of Both RNA and DNA by a Zinc Finger ProteinScience, 1993
- Adjacent zinc-finger motifs in multiple zinc-finger peptides from SWI5 form structurally independent, flexibly linked domainsJournal of Molecular Biology, 1992
- RNA and DNA binding zinc fingers in Xenopus TFIIIACell, 1992
- A finger protein structurally similar to TFIIIA that binds exclusively to 5S RNA in XenopusCell, 1990