title: The MukF subunit of Escherichia coli condensin: architecture and functional relationship to kleisins.
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 A 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.
authors.affiliation: Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720, USA.
authors.forename: Rachel
authors.initials: R
authors.lastname: Fennell-Fezzie
authors.forename: Scott D
authors.initials: SD
authors.lastname: Gradia
authors.forename: David
authors.initials: D
authors.lastname: Akey
authors.forename: James M
authors.initials: JM
authors.lastname: Berger
mesh_terms: D000251:Adenosine Triphosphatases / Q000737:chemistry*; D000595:Amino Acid Sequence; D018797:Cell Cycle Proteins / Q000737:chemistry / Q000502:physiology; D002846:Chromatography, Affinity; D002868:Chromosomal Proteins, Non-Histone / Q000737:chemistry / Q000378:metabolism; D018360:Crystallography, X-Ray; D004268:DNA-Binding Proteins / Q000737:chemistry*; D019281:Dimerization; D004926:Escherichia coli / Q000737:chemistry*; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000378:metabolism / Q000502:physiology; D008958:Models, Molecular; D008969:Molecular Sequence Data; D005810:Multigene Family; D046912:Multiprotein Complexes; D011485:Protein Binding; D011487:Protein Conformation; D025941:Protein Interaction Mapping; D017434:Protein Structure, Tertiary; D012097:Repressor Proteins / Q000737:chemistry / Q000378:metabolism; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D013329:Structure-Activity Relationship
chemical_list: D018797:Cell Cycle Proteins; D002868:Chromosomal Proteins, Non-Histone; D004268:DNA-Binding Proteins; D029968:Escherichia coli Proteins; C067035:MukB protein, E coli; D046912:Multiprotein Complexes; D012097:Repressor Proteins; C108312:condensin complexes; C087115:mukE protein, E coli; C087116:mukF protein, E coli; D000251:Adenosine Triphosphatases