ArticleNucleic acids research2012
Structure and cleavage activity of the tetrameric MspJI DNA modification-dependent restriction endonuclease.
Article in Nucleic acids research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed.
- A bacterial defense system targeting modified cytosine of phage genomic DNA.Nature communications · 2026Article
- Cryo-EM structures of DNA-free and DNA-bound BsaXI: architecture of a Type IIB restriction-modification enzyme.Nucleic acids research · 2025Article
- Ultra-deep whole genome bisulfite sequencing reveals a single methylation hotspot in human brain mitochondrial DNA.Epigenetics · 2022Article
- Coordination of phage genome degradation versus host genome protection by a bifunctional restriction-modification enzyme visualized by CryoEM.Structure (London, England : 1993) · 2021Article
- DNA backbone interactions impact the sequence specificity of DNA sulfur-binding domains: revelations from structural analyses.Nucleic acids research · 2020Article
- The N-terminal domain of Staphylothermus marinus McrB shares structural homology with PUA-like RNA binding proteins.Journal of structural biology · 2020Article
- Structure of HhaI endonuclease with cognate DNA at an atomic resolution of 1.0 Å.Nucleic acids research · 2020Article
- A protein architecture guided screen for modification dependent restriction endonucleases.Nucleic acids research · 2019Article
- Structural basis for the recognition of sulfur in phosphorothioated DNA.Nature communications · 2018Article
- Crystal structure of the modification-dependent SRA-HNH endonuclease TagI.Nucleic acids research · 2018Article
- Activity and structure of EcoKMcrA.Nucleic acids research · 2018Article
- A refined DNA methylation detection method using MspJI coupled quantitative PCR.Analytical biochemistry · 2017Article
- High pressure activation of the Mrr restriction endonuclease in Escherichia coli involves tetramer dissociation.Nucleic acids research · 2017Article
- DNA methylation analysis in malignant pheochromocytoma and paraganglioma.Journal of clinical & translational endocrinology · 2017Article
- DNA Base Flipping: A General Mechanism for Writing, Reading, and Erasing DNA Modifications.Advances in experimental medicine and biology · 2016Review
- Structure-guided sequence specificity engineering of the modification-dependent restriction endonuclease LpnPI.Nucleic acids research · 2015Article
- Recognition and cleavage of 5-methylcytosine DNA by bacterial SRA-HNH proteins.Nucleic acids research · 2015Article
- Modification-dependent restriction endonuclease, MspJI, flips 5-methylcytosine out of the DNA helix.Nucleic acids research · 2014Article
- Structural basis of the methylation specificity of R.DpnI.Nucleic acids research · 2014Article
- Structure of 5-hydroxymethylcytosine-specific restriction enzyme, AbaSI, in complex with DNA.Nucleic acids research · 2014Article
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9 authors.
Funding
Abstract
The MspJI modification-dependent restriction endonuclease recognizes 5-methylcytosine or 5-hydroxymethylcytosine in the context of CNN(G/A) and cleaves both strands at fixed distances (N(12)/N(16)) away from the modified cytosine at the 3'-side. We determined the crystal structure of MspJI of Mycobacterium sp. JLS at 2.05-Å resolution. Each protein monomer harbors two domains: an N-terminal DNA-binding domain and a C-terminal endonuclease. The N-terminal domain is structurally similar to that of the eukaryotic SET and RING-associated domain, which is known to bind to a hemi-methylated CpG dinucleotide. Four protein monomers are found in the crystallographic asymmetric unit. Analytical gel-filtration and ultracentrifugation measurements confirm that the protein exists as a tetramer in solution. Two monomers form a back-to-back dimer mediated by their C-terminal endonuclease domains. Two back-to-back dimers interact to generate a tetramer with two double-stranded DNA cleavage modules. Each cleavage module contains two active sites facing each other, enabling double-strand DNA cuts. Biochemical, mutagenesis and structural characterization suggest three different monomers of the tetramer may be involved respectively in binding the modified cytosine, making the first proximal N(12) cleavage in the same strand and then the second distal N(16) cleavage in the opposite strand. Both cleavage events require binding of at least a second recognition site either in cis or in trans.
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