ArticleNucleic acids research2016
Structural insights into DNA sequence recognition by Type ISP restriction-modification enzymes.
Article in Nucleic acids research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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16 citing papers in PubMed, 21 citations in OpenAlex.
- Lactococcal mobile genetic elements harbour a diverse phage defensome rich in restriction-modification systems.Nucleic acids research · 2025Article
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- Advances in Diversity, Evolutionary Dynamics and Biotechnological Potential of Restriction-Modification Systems.Microorganisms · 2025Review
- Cryo-EM structures of DNA-free and DNA-bound BsaXI: architecture of a Type IIB restriction-modification enzyme.Nucleic acids research · 2025Article
- Molecular basis of foreign DNA recognition by BREX anti-phage immunity system.Nature communications · 2025Article
- Bacterial DNA methyltransferase: A key to the epigenetic world with lessons learned from proteobacteria.Frontiers in microbiology · 2023Review
- Article
- 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
- Structure, subunit organization and behavior of the asymmetric Type IIT restriction endonuclease BbvCI.Nucleic acids research · 2019Article
- A model for the evolution of prokaryotic DNA restriction-modification systems based upon the structural malleability of Type I restriction-modification enzymes.Nucleic acids research · 2018Article
- Engineering altered protein-DNA recognition specificity.Nucleic acids research · 2018Review
- The H-subunit of the restriction endonuclease CglI contains a prototype DEAD-Z1 helicase-like motor.Nucleic acids research · 2018Article
- Structural basis underlying complex assembly and conformational transition of the type I R-M system.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- The third restriction-modification system from Thermus aquaticus YT-1: solving the riddle of two TaqII specificities.Nucleic acids research · 2017Article
- CgII cleaves DNA using a mechanism distinct from other ATP-dependent restriction endonucleases.Nucleic acids research · 2017Article
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
Engineering restriction enzymes with new sequence specificity has been an unaccomplished challenge, presumably because of the complexity of target recognition. Here we report detailed analyses of target recognition by Type ISP restriction-modification enzymes. We determined the structure of the Type ISP enzyme LlaGI bound to its target and compared it with the previously reported structure of a close homologue that binds to a distinct target, LlaBIII. The comparison revealed that, although the two enzymes use almost a similar set of structural elements for target recognition, the residues that read the bases vary. Change in specificity resulted not only from appropriate substitution of amino acids that contacted the bases but also from new contacts made by positionally distinct residues directly or through a water bridge. Sequence analyses of 552 Type ISP enzymes showed that the structural elements involved in target recognition of LlaGI and LlaBIII were structurally well-conserved but sequentially less-conserved. In addition, the residue positions within these structural elements were under strong evolutionary constraint, highlighting the functional importance of these regions. The comparative study helped decipher a partial consensus code for target recognition by Type ISP enzymes.
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