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Discovery of natural nicking endonucleases Nb.BsrDI and Nb.BtsI and engineering of top-strand nicking variants from BsrDI and BtsI

Title: Discovery of natural nicking endonucleases Nb.BsrDI and Nb.BtsI and engineering of top-strand nicking variants from BsrDI and BtsI
Authors: Xu, Shuang-Yong; Zhu, Zhenyu; Zhang, Penghua; Chan, Siu-Hong; Samuelson, James C.; Xiao, Jianping; Ingalls, Debra; Wilson, Geoffrey G.
Publisher Information: Oxford University Press
Publication Year: 2007
Collection: HighWire Press (Stanford University)
Subject Terms: Nucleic Acid Enzymes
Description: BsrDI and BtsI restriction endonucleases recognize and cleave double-strand DNA at the sequences GCAATG (2/0) and GCAGTG (2/0), respectively. We have purified and partially characterized these two enzymes, and analyzed the genes that encode them. BsrDI and BtsI are unusual in two respects: each cleaves DNA as a heterodimer of one large subunit (B subunit) and one small subunit (A subunit); and, in the absence of their small subunits, the large subunits behave as sequence-specific DNA nicking enzymes and only nick the bottom strand of the sequences at these respective positions: GCAATG (−/0) and GCAGTG (−/0). We refer to the single subunit, the bottom-strand nicking forms as ‘hemidimers’. Amino acid sequence comparisons reveal that BsrDI and BtsI belong to a family of restriction enzymes that possess two catalytic sites: a canonical PD-X n -EXK and a second non-canonical PD-X n -E-X 12 -QR. Interestingly, the other family members, which include BsrI (ACTGG 1/−1) and BsmI/Mva1269I (GAATGC 1/−1) are single polypeptide chains, i.e. monomers, rather than heterodimers. In BsrDI and BtsI, the two catalytic sites are found in two separate subunits. Site-directed mutagenesis confirmed that the canonical catalytic site located at the N-terminus of the large subunit is responsible for the bottom-strand cleavage, whereas the non-canonical catalytic site located in the small subunit is responsible for hydrolysis of the top strand. Top-strand specific nicking variants, Nt.BsrDI and Nt.BtsI, were successfully engineered by combining the catalytic-deficient B subunit with wild-type A subunit.
Document Type: text
File Description: text/html
Language: English
Relation: http://nar.oxfordjournals.org/cgi/content/short/gkm481v1; http://dx.doi.org/10.1093/nar/gkm481
DOI: 10.1093/nar/gkm481
Availability: http://nar.oxfordjournals.org/cgi/content/short/gkm481v1; https://doi.org/10.1093/nar/gkm481
Rights: Copyright (C) 2007, Oxford University Press
Accession Number: edsbas.277564B6
Database: BASE