ArticleScientific reports2014
Structure and mutagenesis of the DNA modification-dependent restriction endonuclease AspBHI.
Article in Scientific reports, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 15 citations in OpenAlex.
- The Restriction Activity Investigation of Rv2528c, an Mrr-like Modification-Dependent Restriction Endonuclease fromMicroorganisms · 2024Article
- Recent Advances on DNA Base Flipping: A General Mechanism for Writing, Reading, and Erasing DNA Modifications.Advances in experimental medicine and biology · 2022Article
- The N-terminal domain of Staphylothermus marinus McrB shares structural homology with PUA-like RNA binding proteins.Journal of structural biology · 2020Article
- Protein Domain Guided Screen for Sequence Specific and Phosphorothioate-Dependent Restriction Endonucleases.Frontiers in microbiology · 2020Article
- Structural basis for the recognition of sulfur in phosphorothioated DNA.Nature communications · 2018Article
- Structure of Type IIL Restriction-Modification Enzyme MmeI in Complex with DNA Has Implications for Engineering New Specificities.PLoS biology · 2016Article
- Mechanistic insights into the recognition of 5-methylcytosine oxidation derivatives by the SUVH5 SRA domain.Scientific reports · 2016Article
- 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
- Structure of 5-hydroxymethylcytosine-specific restriction enzyme, AbaSI, in complex with DNA.Nucleic acids research · 2014Article
- Chemical display of pyrimidine bases flipped out by modification-dependent restriction endonucleases of MspJI and PvuRts1I families.PloS one · 2014Article
Corrections and comments
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Authors and funding
12 authors at 2 institutions in 1 country.
Funding
Abstract
The modification-dependent restriction endonuclease AspBHI recognizes 5-methylcytosine (5mC) in the double-strand DNA sequence context of (C/T)(C/G)(5mC)N(C/G) (N = any nucleotide) and cleaves the two strands a fixed distance (N12/N16) 3' to the modified cytosine. We determined the crystal structure of the homo-tetrameric AspBHI. Each subunit of the protein comprises two domains: an N-terminal DNA-recognition domain and a C-terminal DNA cleavage domain. The N-terminal domain is structurally similar to the eukaryotic SET and RING-associated (SRA) domain, which is known to bind to a hemi-methylated CpG dinucleotide. The C-terminal domain is structurally similar to classic Type II restriction enzymes and contains the endonuclease catalytic-site motif of DX20EAK. To understand how specific amino acids affect AspBHI recognition preference, we generated a homology model of the AspBHI-DNA complex, and probed the importance of individual amino acids by mutagenesis. Ser41 and Arg42 are predicted to be located in the DNA minor groove 5' to the modified cytosine. Substitution of Ser41 with alanine (S41A) and cysteine (S41C) resulted in mutants with altered cleavage activity. All 19 Arg42 variants resulted in loss of endonuclease activity.
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