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Updated: Aug 13, 2026
11:24
Direct Protein Delivery to Mammalian Cells Using Cell-permeable Cys2-His2 Zinc-finger Domains
Published on: March 25, 2015
Designer zinc finger proteins: tools for creating artificial DNA-binding functional proteins
Muthu Dhanasekaran1, Shigeru Negi, Yukio Sugiura
1Faculty of Pharmaceutical Sciences, Doshisha Women's University, Koudo, Kyotanabe-Shi, Kyoto 610 0395, Japan.
Accounts of Chemical Research
|January 18, 2006
Summary
Researchers engineered novel zinc finger peptides by redesigning Sp1 transcription factor
Area of Science:
- Biochemistry
- Molecular Biology
- Protein Engineering
Background:
- Artificial DNA-binding proteins are crucial for molecular biology research.
- Zinc finger proteins are extensively studied for their DNA recognition capabilities.
- The tandem arrangement of zinc fingers offers a versatile framework for protein design.
Purpose of the Study:
- To design novel artificial DNA-binding peptides.
- To re-engineer the C(2)H(2)-type zinc finger motif of transcription factor Sp1.
- To explore the functional properties of engineered zinc fingers.
Main Methods:
- Utilized several design strategies for protein engineering.
- Focused on re-engineering the C(2)H(2)-type zinc finger motif.
- Employed Sp1 transcription factor as a base motif.
Main Results:
- Successfully created novel zinc finger peptides.
- Some engineered zinc fingers exhibited nuclease activity.
- Other engineered variants displayed catalytic functional properties.
Conclusions:
- The C(2)H(2)-type zinc finger motif of Sp1 can be re-engineered to create novel functional proteins.
- Engineered zinc fingers show potential for nuclease and catalytic applications.
- Design strategies presented offer a pathway for creating custom DNA-binding proteins.
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