Site-specific DNA cleavage by artificial zinc finger-type nuclease with cerium-binding peptide

Journal Article · Fri Apr 29 00:00:00 EDT 2005 · Biochemical and Biophysical Research Communications

DOI:https://doi.org/10.1016/j.bbrc.2005.02.164· OSTI ID:20709162

Nakatsukasa, Takako ^[1]; Shiraishi, Yasuhisa ^[1]; Negi, Shigeru ^[1]; Imanishi, Miki ^[1]; Futaki, Shiroh ^[1]; Sugiura, Yukio ^[1]

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1. Institute for Chemical Research, Kyoto University, Uji, Kyoto 611-0011 (Japan)

The addition of a new function to native proteins is one of the most attractive protein-based designs. In this study, we have converted a C{sub 2}H{sub 2}-type zinc finger as a DNA-binding motif into a novel zinc finger-type nuclease by connecting two distinct zinc finger proteins (Sp1 and GLI) with a functional linker possessing DNA cleavage activity. As a DNA cleavage domain, we chose an analogue of the metal-binding loop (12 amino acid residues), peptide P1, which has been reported to exhibit a strong binding affinity for a lanthanide ion and DNA cleavage ability in the presence of Ce(IV). Our newly designed nucleases, Sp1(P1)GLI and Sp1(P1G)GLI, can strongly bind to a lanthanide ion and show a unique DNA cleavage pattern, in which certain positions between the two DNA-binding sites are specifically cleaved. The present result provides useful information for expanding the design strategy for artificial nucleases.

• OSTI ID: 20709162
• Journal Information: Biochemical and Biophysical Research Communications, Vol. 330, Issue 1; Other Information: DOI: 10.1016/j.bbrc.2005.02.164; PII: S0006-291X(05)00442-0; Copyright (c) 2005 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA); ISSN 0006-291X
• Country of Publication: United States
• Language: English

Related Subjects

60 APPLIED LIFE SCIENCES
ACETYLENE
AFFINITY
AMINO ACIDS
CALCIUM
CERIUM
CLEAVAGE
DNA
NUCLEASES
PEPTIDES
ZINC