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  • Title: Biochemical and mutational analysis of EcoRII functional domains reveals evolutionary links between restriction enzymes.
    Author: Tamulaitis G, Mucke M, Siksnys V.
    Journal: FEBS Lett; 2006 Mar 06; 580(6):1665-71. PubMed ID: 16497303.
    Abstract:
    The archetypal Type IIE restriction endonuclease EcoRII is a dimer that has a modular structure. DNA binding studies indicate that the isolated C-terminal domain dimer has an interface that binds a single cognate DNA molecule whereas the N-terminal domain is a monomer that also binds a single copy of cognate DNA. Hence, the full-length EcoRII contains three putative DNA binding interfaces: one at the C-terminal domain dimer and two at each of the N-terminal domains. Mutational analysis indicates that the C-terminal domain shares conserved active site architecture and DNA binding elements with the tetrameric restriction enzyme NgoMIV. Data provided here suggest possible evolutionary relationships between different subfamilies of restriction enzymes.
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