Chemistry: molecular biology and microbiology – Enzyme – proenzyme; compositions thereof; process for... – Hydrolase
Patent
1996-05-07
1999-06-29
Housel, James C.
Chemistry: molecular biology and microbiology
Enzyme , proenzyme; compositions thereof; process for...
Hydrolase
435193, 435 697, 435 691, 536 231, 536 232, C12N 922, C12N 910, C07H 2102, C07H 2104
Patent
active
059167947
ABSTRACT:
The present invention reveals a method for enzymatically inactivating a target DNA, a method for detecting conformational change in a nucleic acid, and a method for detecting the presence of a target DNA molecule. The method for enzymatically inactivating a target DNA involves preparing a plasmid, phage, virus, or any other delivery vehicle such as a liposome containing a gene encoding a nuclease. The delivery vehicle is then delivered into cells. The cells are induced to produce the nuclease and the target DNA is then enzymatically inactivated. Alternatively, the nuclease protein is delivered directly to cells and used to enzymatically inactivate the target DNA. The method for detecting conformational change in a nucleic acid requires contacting a nucleic acid with a hybrid restriction nuclease, determining whether the hybrid restriction nuclease has interacted with the nucleic acid, and detecting the conformational change in the nucleic acid. The method for detecting the presence of a target DNA entails contacting a target DNA with a fusion protein, comprising a DNA binding protein joined to a detection domain such as the constant region of an immunoglogulin heavy chain molecule.
REFERENCES:
patent: 5356802 (1994-10-01), Chandrasegaran
patent: 5436150 (1995-07-01), Chandrasegaran
Dako Corporation, "1993 Catalog/Price List", pp. 119-125, Jan. 1, 1993.
Rima Youil et al., Screening for Mutations by Enzyme Mismatch Cleavage with T4 Endonuclease VII, Proc. Natl. Acad. Sci. USA, Jan. 1995, pp. 87-91, vol. 92.
Alla Lishanski et al., Mutation Detection by Mismatch Binding Protein, MutS, in Amplified DNA: Application to the Cystic Fibrosis Gene, Proc. Natl. Acad. Sci. USA, Mar. 1994, pp. 2674-2678, vol. 91.
Adrian Whitehouse et al., A Carboxy Terminal Domain of the hMSH-2 Gene Product is Sufficient for Binding Specific Mismatched Oligonucleotides, Biochemical and Biophysical Research Communications, 1996, vol. 225, 289-295, Article No. 1168.
Yang-Gyun Kim et al., Hybrid Restriction Enzymes: Zinc Finger Fusions to FOK I Cleavage Domain, Proc. Natl. Acad. Sci. USA, Feb. 1996, 1156-1160, vol. 93.
Yang-Gyun Kim et al., Chimeric Restriction Endonuclease, Pro. Natl. Acad. Sci. USA, Feb. 1994, pp. 883-887, vol. 91.
Lin Li et al., Functional Domains in Fok I Restriction Endonuclease, Proc. Natl. Acad. Sci. USA, May 1992, pp. 4275-4279, vol. 89.
Lin Li et al., C-terminal Deletion Mutants of the Fok I Restriction Endonuclease, Gene, 133 1993, pp. 79-84.
Lin Li et al., Alteration of the Cleavage Distance of Fok I Restriction Endonuclease by Insertion Mutagenesis, Pro. Natl. Acad. Sci, USA, Apr. 1993, pp. 2764-2768, vol. 90.
Yang-Gyun Kim et al., Insertion and Deletion Mutants of Fok I Restriction Endonuclease, The Journal of Biological Chemistry, Dec. 16, 1994, pp. 31978-31982, vol. 269, No. 50.
Baohua Huang et al., Splase: A New Class IIS Zinc-Finger Restriction Endonuclease with Specificity for Sp1 Binding Sites, Journal of Protein Chemistry, 1996, pp. 481-489, vol. 15.
Yen Choo et al., In Vivo Repression by a Site-Specific DNA-Binding Protein Designed Against an Oncogenic Sequence, Nature, Dec. 15, 1994, pp. 642-645, vol. 372.
Housel James C.
Johns Hopkins University
Swartz Rodney P.
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