A view of consecutive binding events from structures of tetrameric endonuclease SfiI bound to DNA

Éva Scheuring Vanamee, Hector Viadiu, Rebecca Kucera, Lydia Dorner, Stephen Picone, Ira Schildkraut, Aneel K. Aggarwal

Research output: Contribution to journalArticlepeer-review

50 Scopus citations

Abstract

Many reactions in cells proceed via the sequestration of two DNA molecules in a synaptic complex. SfiI is a member of a growing family of restriction enzymes that can bind and cleave two DNA sites simultaneously. We present here the structures of tetrameric SfiI in complex with cognate DNA. The structures reveal two different binding states of SfiI: one with both DNA-binding sites fully occupied and the other with fully and partially occupied sites. These two states provide details on how SfiI recognizes and cleaves its target DNA sites, and gives insight into sequential binding events. The SfiI recognition sequence (GGCCNNNN ↓ NGGCC) is a subset of the recognition sequence of BglI (GCCNNNN ↓ NGGC), and both enzymes cleave their target DNAs to leave 3-base 3′ overhangs. We show that even though SfiI is a tetramer and BglI is a dimer, and there is little sequence similarity between the two enzymes, their modes of DNA recognition are unusually similar.

Original languageEnglish
Pages (from-to)4198-4208
Number of pages11
JournalEMBO Journal
Volume24
Issue number23
DOIs
StatePublished - 7 Dec 2005

Keywords

  • Protein/DNA complex
  • Specific DNA cleavage
  • Type IIF restriction endonuclease

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