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The link between restriction endonuclease fidelity and oligomeric state: A study with Bse634I
Author(s) -
Zaremba Mindaugas,
Sasnauskas Giedrius,
Siksnys Virginijus
Publication year - 2012
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2012.07.009
Subject(s) - restriction enzyme , cleavage (geology) , dna , fidelity , endonuclease , biophysics , chemistry , biology , genetics , computational biology , computer science , paleontology , telecommunications , fracture (geology)
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.