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Direct Protein Delivery to Mammalian Cells Using Cell-permeable Cys2-His2 Zinc-finger Domains
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Iron-Sulfur Clusters in Zinc Finger Proteins
Geoffrey D Shimberg1, Jordan D Pritts1, Sarah L J Michel1
1School of Pharmacy, University of Maryland, Baltimore, MD, United States.
Methods in Enzymology
|May 11, 2018
Summary
This study details methods for isolating and characterizing the zinc finger protein, cleavage and polyadenylation specificity factor 30 (CPSF3O). We investigate its metal-binding properties and RNA interactions, revealing insights into alternative metal cofactors.
Area of Science:
- Biochemistry
- Molecular Biology
- Proteomics
Background:
- Zinc finger (ZF) proteins utilize zinc as a structural cofactor, typically with cysteine or histidine residues.
- Genome sequencing led to broad annotation of ZF proteins, but experimental characterization revealed some utilize iron-sulfur clusters instead of or alongside zinc.
Purpose of the Study:
- To describe methods for isolating and characterizing a specific ZF protein, cleavage and polyadenylation specificity factor 30 (CPSF3O).
- To investigate the metal-loading and RNA-binding activities of CPSF3O.
Main Methods:
- Isolation of the CPSF3O protein.
- Characterization of metal-binding capabilities.
- Assessment of RNA-binding activity.
Main Results:
- Successful isolation and characterization of CPSF3O.
- Detailed analysis of its metal-binding properties.
- Evaluation of its functional RNA-binding activity.
Conclusions:
- CPSF3O can be isolated and characterized using the described methods.
- The study provides insights into the metal-loading and RNA-binding functions of this specific zinc finger protein, highlighting the diversity of cofactor usage in ZFs.
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