ArticleNucleic acids research2013
The Type ISP Restriction-Modification enzymes LlaBIII and LlaGI use a translocation-collision mechanism to cleave non-specific DNA distant from their recognition sites.
Article in Nucleic acids research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 15 citations in OpenAlex.
- New Platform for Screening Genetic Libraries at Elevated Temperatures: Biological and Genomic Information and Genetic Tools of Geobacillus thermodenitrificans K1041.Applied and environmental microbiology · 2022Article
- ENDO-Pore: high-throughput linked-end mapping of single DNA cleavage events using nanopore sequencing.Nucleic acids research · 2021Article
- Coordination of phage genome degradation versus host genome protection by a bifunctional restriction-modification enzyme visualized by CryoEM.Structure (London, England : 1993) · 2021Article
- DNA-mediated coupling of ATPase, translocase and nuclease activities of a Type ISP restriction-modification enzyme.Nucleic acids research · 2020Article
- The Ability of Lytic Staphylococcal Podovirus vB_SauP_phiAGO1.3 to Coexist in Equilibrium With Its Host Facilitates the Selection of Host Mutants of Attenuated Virulence but Does Not Preclude the Phage Antistaphylococcal Activity in a Nematode Infection Model.Frontiers in microbiology · 2018Article
- CgII cleaves DNA using a mechanism distinct from other ATP-dependent restriction endonucleases.Nucleic acids research · 2017Article
- Structural insights into DNA sequence recognition by Type ISP restriction-modification enzymes.Nucleic acids research · 2016Article
- Mapping DNA cleavage by the Type ISP restriction-modification enzymes following long-range communication between DNA sites in different orientations.Nucleic acids research · 2015Article
- Translocation-coupled DNA cleavage by the Type ISP restriction-modification enzymes.Nature chemical biology · 2015Article
- TstI, a Type II restriction-modification protein with DNA recognition, cleavage and methylation functions in a single polypeptide.Nucleic acids research · 2014Article
- Type I restriction enzymes and their relatives.Nucleic acids research · 2014Review
- DNA cleavage by Type ISP Restriction-Modification enzymes is initially targeted to the 3'-5' strand.Nucleic acids research · 2013Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The Type ISP Restriction-Modification (RM) enzyme LlaBIII is encoded on plasmid pJW566 and can protect Lactococcus lactis strains against bacteriophage infections in milk fermentations. It is a single polypeptide RM enzyme comprising Mrr endonuclease, DNA helicase, adenine methyltransferase and target-recognition domains. LlaBIII shares >95% amino acid sequence homology across its first three protein domains with the Type ISP enzyme LlaGI. Here, we determine the recognition sequence of LlaBIII (5'-TnAGCC-3', where the adenine complementary to the underlined base is methylated), and characterize its enzyme activities. LlaBIII shares key enzymatic features with LlaGI; namely, adenosine triphosphate-dependent DNA translocation (∼309 bp/s at 25°C) and a requirement for DNA cleavage of two recognition sites in an inverted head-to-head repeat. However, LlaBIII requires K(+) ions to prevent non-specific DNA cleavage, conditions which affect the translocation and cleavage properties of LlaGI. By identifying the locations of the non-specific dsDNA breaks introduced by LlaGI or LlaBIII under different buffer conditions, we validate that the Type ISP RM enzymes use a common translocation-collision mechanism to trigger endonuclease activity. In their favoured in vitro buffer, both LlaGI and LlaBIII produce a normal distribution of random cleavage loci centred midway between the sites. In contrast, LlaGI in K(+) ions produces a far more distributive cleavage profile.
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