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Updated: Jun 2, 2026

12:03
Protocols for C-Brick DNA Standard Assembly Using Cpf1
Published on: June 15, 2017
Engineering of a redox protein for DNA-directed assembly
Géza R Szilvay1, Shayna Brocato, Dmitri Ivnitski
1Department of Chemical Engineering, Columbia University, 500 W 120th Street, New York, NY 10027, USA. geza.szilvay@vtt.fi
Summary
Engineered enzymes can now bind specific DNA sites. This conjugate retains its enzymatic activity for targeted applications.
Area of Science:
- Biochemistry
- Molecular Biology
- Enzyme Engineering
Background:
- Site-specific DNA binding is crucial for gene regulation and biotechnology.
- Developing novel DNA-binding proteins with retained enzymatic function presents challenges.
Purpose of the Study:
- To engineer a novel enzyme-DNA binding conjugate.
- To assess the DNA binding specificity and enzymatic activity of the conjugate.
Main Methods:
- Conjugation of a small laccase enzyme from Streptomyces coelicolor with a zinc finger DNA binding domain (Zif268).
- Characterization of the conjugate's ability to bind double-stranded DNA.
- Assay of the conjugate's enzymatic activity post-conjugation.
Main Results:
- The engineered enzyme conjugate successfully bound double-stranded DNA.
- DNA binding was demonstrated to be site-specific.
- The conjugate retained its native enzymatic activity after conjugation.
Conclusions:
- The engineered enzyme conjugate represents a novel tool for site-specific DNA targeting.
- This approach combines DNA recognition with enzymatic function for potential biotechnological applications.
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