ArticleNucleic acids research2007
Discovery of natural nicking endonucleases Nb.BsrDI and Nb.BtsI and engineering of top-strand nicking variants from BsrDI and BtsI.
Article in Nucleic acids research, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 53 citations in OpenAlex.
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- Strand-selective base editing of human mitochondrial DNA using mitoBEs.Nature biotechnology · 2024Article
- Robust and scalable barcoding for massively parallel long-read sequencing.Scientific reports · 2022Article
- Types and Applications of Nicking Enzyme-Combined Isothermal Amplification.International journal of molecular sciences · 2022Review
- Cleavage-free human genome editing.Molecular therapy : the journal of the American Society of Gene Therapy · 2022Article
- A nucleotide-sensing endonuclease from the Gabija bacterial defense system.Nucleic acids research · 2021Article
- Engineering Infrequent DNA Nicking Endonuclease by Fusion of aFrontiers in microbiology · 2021Article
- A molecular device: A DNA molecular lock driven by the nicking enzymes.Computational and structural biotechnology journal · 2020Article
- A protein architecture guided screen for modification dependent restriction endonucleases.Nucleic acids research · 2019Article
- Colorimetric detection of nucleic acid sequences in plant pathogens based on CRISPR/Cas9 triggered signal amplification.Mikrochimica acta · 2019Article
- Structure, subunit organization and behavior of the asymmetric Type IIT restriction endonuclease BbvCI.Nucleic acids research · 2019Article
- Restriction and modification of deoxyarchaeosine (dGScientific reports · 2017Article
- Type II restriction endonucleases--a historical perspective and more.Nucleic acids research · 2014Review
- Engineering nicking enzymes that preferentially nick 5-methylcytosine-modified DNA.Nucleic acids research · 2014Article
- Massively parallel characterization of restriction endonucleases.Nucleic acids research · 2013Article
- Site- and strand-specific nicking of DNA by fusion proteins derived from MutH and I-SceI or TALE repeats.Nucleic acids research · 2013Article
- Natural zinc ribbon HNH endonucleases and engineered zinc finger nicking endonuclease.Nucleic acids research · 2013Article
- DNA fragments assembly based on nicking enzyme system.PloS one · 2013Article
- Versatile design and synthesis platform for visualizing genomes with Oligopaint FISH probes.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Characterization of type II and III restriction-modification systems from Bacillus cereus strains ATCC 10987 and ATCC 14579.Journal of bacteriology · 2012Article
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Authors and funding
8 authors at 1 institution in 1 country.
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Abstract
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-X12-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.
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