Work

Structure of Fok I has implications for DNA cleavage

Year: 1998

Type: article

Abstract: FokI is a member an unusual class of restriction enzymes that recognize a specific DNA sequence and cleave nonspecifically a short distance away from that sequence. FokI consists of an N-terminal DNA recognition domain and a C-terminal cleavage domain. The bipartite nature of FokI has led to the development of artificial enzymes with novel specificities. We have solved the structure of FokI to 2.3 A resolution. The structure reveals a dimer, in which the dimerization interface is mediated by the cleavage domain. Each monomer has an overall conformation similar to that found in the FokI-DNA complex, with the cleavage domain packing alongside the DNA recognition domain. In corroboration with the cleavage data presented in the accompanying paper in this issue of Proceedings, we propose a model for FokI DNA cleavage that requires the dimerization of FokI on DNA to cleave both DNA strands.

Source: Proceedings of the National Academy of Sciences

DOI: 10.1073/pnas.95.18.10564

Authors: David A. Wah, Jurate Bitinaite, Ira Schildkraut, Aneel K. Aggarwal

Institution: Icahn School of Medicine at Mount Sinai

Language: English

Topic: CRISPR and Genetic Engineering

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: green

Funders: National Institutes of Health, National Eye Institute, National Institute of General Medical Sciences

Awards: TRAINING FOR CAREERS IN MOLECULAR OPHTHALMOLOGY, Recognition and Cleavage of DNA by Restriction Enzymes