The MukF subunit of Escherichia coli condensin: Architecture and functional relationship to kleisins

Rachel Fennell-Fezzie, Scott D. Gradia, David Akey, James M. Berger

Research output: Contribution to journalArticlepeer-review

Abstract

The Escherichia coli MukB, MukE, and MukF proteins form a bacterial condensin (MukBEF) that contributes to chromosome management by compacting DNA. MukB is an ATPase and DNA-binding protein of the SMC superfamily; however, the structure and function of non-SMC components, such as MukF, have been less forthcoming. Here, we report the crystal structure of the N-terminal 287 amino acids of MukF at 2.9 Å resolution. This region folds into a winged-helix domain and an extended coiled-coil domain that self-associate to form a stable, doubly domain-swapped dimer. Protein dissection and affinity purification data demonstrate that the region of MukF C-terminal to this fragment binds to MukE and MukB. Our findings, together with sequence analyses, indicate that MukF is a kleisin subunit for E. coli condensin and suggest a means by which it may organize the MukBEF assembly.

Original languageEnglish (US)
Pages (from-to)1921-1930
Number of pages10
JournalEMBO Journal
Volume24
Issue number11
DOIs
StatePublished - Jun 1 2005
Externally publishedYes

Keywords

  • Chromosome structure
  • Cohesin
  • Condensin
  • Muk
  • SMC

ASJC Scopus subject areas

  • Neuroscience(all)
  • Molecular Biology
  • Biochemistry, Genetics and Molecular Biology(all)
  • Immunology and Microbiology(all)

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