Biochemical and mutational analysis of Eco RII functional domains reveals evolutionary links between restriction enzymes

The archetypal Type IIE restriction endonuclease Eco RII 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...

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Bibliographic Details
Published inFEBS letters Vol. 580; no. 6; pp. 1665 - 1671
Main Authors Tamulaitis, Gintautas, Mucke, Merlind, Siksnys, Virginijus
Format Journal Article
LanguageEnglish
Published 06.03.2006
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Summary:The archetypal Type IIE restriction endonuclease Eco RII 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 Eco RII 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 Ngo MIV. Data provided here suggest possible evolutionary relationships between different subfamilies of restriction enzymes.
ISSN:0014-5793
1873-3468
DOI:10.1016/j.febslet.2006.02.010