ArticlePloS one2011
Structure of HsdS subunit from Thermoanaerobacter tengcongensis sheds lights on mechanism of dynamic opening and closing of type I methyltransferase.
Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Molecular insights into DNA recognition and methylation by non-canonical type I restriction-modification systems.Nature communications · 2022Article
- Genetically distant bacteriophages select for unique genomic changes in Enterococcus faecalis.MicrobiologyOpen · 2022Article
- Improving Mobilization of Foreign DNA into Zymomonas mobilis Strain ZM4 by Removal of Multiple Restriction Systems.Applied and environmental microbiology · 2021Article
- Structural insights into assembly, operation and inhibition of a type I restriction-modification system.Nature microbiology · 2020Article
- Crystal structure of a novel domain of the motor subunit of the Type I restriction enzyme EcoR124 involved in complex assembly and DNA binding.The Journal of biological chemistry · 2018Article
- 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
- Article
- 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
- Cloning, crystallization and preliminary X-ray diffraction analysis of an intact DNA methyltransferase of a type I restriction-modification enzyme from Vibrio vulnificus.Acta crystallographica. Section F, Structural biology communications · 2014Article
- Type I restriction enzymes and their relatives.Nucleic acids research · 2014Review
- Impact of target site distribution for Type I restriction enzymes on the evolution of methicillin-resistant Staphylococcus aureus (MRSA) populations.Nucleic acids research · 2013Article
- Removal of a frameshift between the hsdM and hsdS genes of the EcoKI Type IA DNA restriction and modification system produces a new type of system and links the different families of Type I systems.Nucleic acids research · 2012Article
- Structural and functional analysis of the symmetrical Type I restriction endonuclease R.EcoR124IPloS one · 2012Article
- Structure and operation of the DNA-translocating type I DNA restriction enzymes.Genes & development · 2012Article
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5 authors.
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Abstract
Type I DNA methyltransferases contain one specificity subunit (HsdS) and two modification subunits (HsdM). The electron microscopy model of M.EcoKI-M₂S₁ methyltransferase shows a reasonable closed state of this clamp-like enzyme, but the structure of the open state is still unclear. The 1.95 Å crystal structure of the specificity subunit from Thermoanaerobacter tengcongensis (TTE-HsdS) shows an unreported open form inter-domain orientation of this subunit. Based on the crystal structure of TTE-HsdS and the closed state model of M.EcoKI-M₂S₁, we constructed a potential open state model of type I methyltransferase. Mutational studies indicated that two α-helices (aa30-59 and aa466-495) of the TTE-HsdM subunit are important inter-subunit interaction sites in the TTE-M₂S₁ complex. DNA binding assays also highlighted the importance of the C-terminal region of TTE-HsdM for DNA binding by the TTE-M₂S₁ complex. On the basis of structural analysis, biochemical experiments and previous studies, we propose a dynamic opening and closing mechanism for type I methyltransferase.
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