Splase: A new class IIs zinc-finger restriction endonuclease with specificity for Sp1 binding sites View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1996-07

AUTHORS

Baohua Huang, Christopher J. Schaeffer, Qunhui Li, Ming-Daw Tsai

ABSTRACT

A new restriction endonuclease, named Splase, was constructed by genetically fusing the DNA-cleavage domain of the restriction endonuclease Fok1 with the zinc-finger DNA-binding domain of the transcription factor Sp1. The resulting protein was expressed in Escherichia coli., partially purified, and shown to selectively digest plasmid DNA harboring consensus Sp1 sites. Splase was also shown to selectively digest the long terminal repeat of the HIV-1 DNA at Sp1 sites. Splase recognizes a 10-bp DNA sequence and hydrolyzes phosphodiester bonds upstream of the binding sequence. The binding specificity of Splase makes this a "rare cutter" restriction enzyme which could be valuable in creating large DNA fragments for genome sequencing projects. The result also presents the opportunity to create other restriction enzymes by altering the binding specificity of the zinc-finger recognition helix. More... »

PAGES

481-489

Journal

TITLE

The Protein Journal

ISSUE

5

VOLUME

15

Author Affiliations

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/bf01886856

DOI

http://dx.doi.org/10.1007/bf01886856

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1036882003

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/8895094


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