ArticlePLoS biology2016
Structure of Type IIL Restriction-Modification Enzyme MmeI in Complex with DNA Has Implications for Engineering New Specificities.
Article in PLoS biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 30 citations in OpenAlex.
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- Structure and rational engineering of the PglX methyltransferase and specificity factor for BREX phage defence.Nature communications · 2024Article
- Symmetric and asymmetric DNA N6-adenine methylation regulates different biological responses in Mucorales.Nature communications · 2024Article
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- Bat Use of Hollows in California's Old-Growth Redwood Forests: From DNA to Ecology.Animals : an open access journal from MDPI · 2022Article
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- Coordination of phage genome degradation versus host genome protection by a bifunctional restriction-modification enzyme visualized by CryoEM.Structure (London, England : 1993) · 2021Article
- A nucleotide-sensing endonuclease from the Gabija bacterial defense system.Nucleic acids research · 2021Article
- Mechanism of DNA cleavage by the endonuclease SauUSI: a major barrier to horizontal gene transfer and antibiotic resistance in Staphylococcus aureus.Nucleic acids research · 2021Article
- Phage T7 DNA mimic protein Ocr is a potent inhibitor of BREX defence.Nucleic acids research · 2020Article
- A Novel Bacteriophage Exclusion (BREX) System Encoded by theApplied and environmental microbiology · 2019Article
- 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
- Digestion-ligation-only Hi-C is an efficient and cost-effective method for chromosome conformation capture.Nature genetics · 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
- DNA target recognition domains in the Type I restriction and modification systems of Staphylococcus aureus.Nucleic acids research · 2017Article
Corrections and comments
- Erratum issued
Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
The creation of restriction enzymes with programmable DNA-binding and -cleavage specificities has long been a goal of modern biology. The recently discovered Type IIL MmeI family of restriction-and-modification (RM) enzymes that possess a shared target recognition domain provides a framework for engineering such new specificities. However, a lack of structural information on Type IIL enzymes has limited the repertoire that can be rationally engineered. We report here a crystal structure of MmeI in complex with its DNA substrate and an S-adenosylmethionine analog (Sinefungin). The structure uncovers for the first time the interactions that underlie MmeI-DNA recognition and methylation (5'-TCCRAC-3'; R = purine) and provides a molecular basis for changing specificity at four of the six base pairs of the recognition sequence (5'-TCCRAC-3'). Surprisingly, the enzyme is resilient to specificity changes at the first position of the recognition sequence (5'-TCCRAC-3'). Collectively, the structure provides a basis for engineering further derivatives of MmeI and delineates which base pairs of the recognition sequence are more amenable to alterations than others.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.