ArticleNucleic acids research2014
Structural insight into the specificity of the B3 DNA-binding domains provided by the co-crystal structure of the C-terminal fragment of BfiI restriction enzyme.
Article in Nucleic acids research, 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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13 citing papers in PubMed, 23 citations in OpenAlex.
- Unveiling the multifaceted domain polymorphism of the Menshen antiphage system.Nucleic acids research · 2025Article
- smFRET Detection of Cis and Trans DNA Interactions by the BfiI Restriction Endonuclease.The journal of physical chemistry. B · 2023Article
- Crystal Structure of a Phospholipase D from the Plant-Associated BacteriaInternational journal of molecular sciences · 2021Article
- Evolution of the Auxin Response Factors from charophyte ancestors.PLoS genetics · 2019Article
- Evolution and conservation of polycomb repressive complex 1 core components and putative associated factors in the green lineage.BMC genomics · 2019Article
- The crystal structure of theThe Journal of biological chemistry · 2018Article
- Structural basis of DNA target recognition by the B3 domain of Arabidopsis epigenome reader VAL1.Nucleic acids research · 2018Article
- UbaLAI is a monomeric Type IIE restriction enzyme.Nucleic acids research · 2017Article
- Deciphering the Molecular Mechanisms Underpinning the Transcriptional Control of Gene Expression by Master Transcriptional Regulators in Arabidopsis Seed.Plant physiology · 2016Article
- Characterization and functional analysis of a B3 domain factor from Zea mays.Journal of applied genetics · 2015Article
- DNA cleavage by CgII and NgoAVII requires interaction between N- and R-proteins and extensive nucleotide hydrolysis.Nucleic acids research · 2014Article
- Crystal structure of the R-protein of the multisubunit ATP-dependent restriction endonuclease NgoAVII.Nucleic acids research · 2014Article
- Type II restriction endonucleases--a historical perspective and more.Nucleic acids research · 2014Review
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7 authors at 1 institution in 1 country.
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Abstract
The B3 DNA-binding domains (DBDs) of plant transcription factors (TF) and DBDs of EcoRII and BfiI restriction endonucleases (EcoRII-N and BfiI-C) share a common structural fold, classified as the DNA-binding pseudobarrel. The B3 DBDs in the plant TFs recognize a diverse set of target sequences. The only available co-crystal structure of the B3-like DBD is that of EcoRII-N (recognition sequence 5'-CCTGG-3'). In order to understand the structural and molecular mechanisms of specificity of B3 DBDs, we have solved the crystal structure of BfiI-C (recognition sequence 5'-ACTGGG-3') complexed with 12-bp cognate oligoduplex. Structural comparison of BfiI-C-DNA and EcoRII-N-DNA complexes reveals a conserved DNA-binding mode and a conserved pattern of interactions with the phosphodiester backbone. The determinants of the target specificity are located in the loops that emanate from the conserved structural core. The BfiI-C-DNA structure presented here expands a range of templates for modeling of the DNA-bound complexes of the B3 family of plant TFs.
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