title: The link between restriction endonuclease fidelity and oligomeric state: a study with Bse634I.
abstract: Type II restriction endonucleases (REases) exist in multiple oligomeric forms. The tetrameric REases have two DNA binding interfaces and must synapse two recognition sites to achieve cleavage. It was hypothesised that binding of two recognition sites by tetrameric enzymes contributes to their fidelity. Here, we experimentally determined the fidelity for Bse634I REase in different oligomeric states. Surprisingly, we find that tetramerisation does not increase REase fidelity in comparison to the dimeric variant. Instead, an inherent ability to act concertedly at two sites provides tetrameric REase with a safety-catch to prevent host DNA cleavage if a single unmodified site becomes available.
authors: Institute of Biotechnology, Vilnius University, Vilnius, Lithuania.
authors: Mindaugas
authors: M
authors: Zaremba
authors: Giedrius
authors: G
authors: Sasnauskas
authors: Virginijus
authors: V
authors: Siksnys
mesh_terms: D000494:Allosteric Regulation; D019943:Amino Acid Substitution; D010582:Bacteriophage lambda / Q000235:genetics / Q000378:metabolism; D001483:Base Sequence; D020134:Catalytic Domain; D004279:DNA, Viral / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D015252:Deoxyribonucleases, Type II Site-Specific / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D016297:Mutagenesis, Site-Directed; D010957:Plasmids / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D055503:Protein Multimerization; D020836:Protein Structure, Quaternary; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism
chemical_list: D004279:DNA, Viral; D011994:Recombinant Proteins; D015252:Deoxyribonucleases, Type II Site-Specific