Zinc finger proteins: getting a grip on RNA
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Updated: Aug 19, 2026

Optical Tweezers to Study RNA-Protein Interactions in Translation Regulation
Published on: February 12, 2022
1Division of Experimental Medicine, Beth Israel Deaconess Medical Center, Harvard Institutes of Medicine, 4 Blackfan Circle, Boston, MA 02115, USA. rbrown7@bidmc.harvard.edu
Abstract:
C2H2 (Cys-Cys-His-His motif) zinc finger proteins are members of a large superfamily of nucleic-acid-binding proteins in eukaryotes. On the basis of NMR and X-ray structures, we know that DNA sequence recognition involves a short alpha helix bound to the major groove. Exactly how some zinc finger proteins bind to double-stranded RNA has been a complete mystery for over two decades. This has been resolved by the long-awaited crystal structure of part of the TFIIIA-5S RNA complex. A comparison can be made with identical fingers in a TFIIIA-DNA structure. Additionally, the NMR structure of TIS11d bound to an AU-rich element reveals the molecular details of the interaction between CCCH fingers and single-stranded RNA. Together, these results contrast the different ways that zinc finger proteins bind with high specificity to their RNA targets.
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