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The MukF subunit of Escherichia coli condensin: architecture and functional relationship to kleisins
Author(s) -
FennellFezzie Rachel,
Gradia Scott D,
Akey David,
Berger James M
Publication year - 2005
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1038/sj.emboj.7600680
Subject(s) - condensin , biology , escherichia coli , protein subunit , dna , coiled coil , microbiology and biotechnology , genetics , chromosome , chromosome segregation , gene
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.